Variants of the Alpha Chain

References

• Crookston J. H., Beale D., Irvine D., Lehmann H. A new Haemoglobin J Toronto (α5 AlanineAspartic acid). Nature 1965; 208: 1059
   PubMed Web of Science ®Google Scholar
• Sumida I., Ohta Y., Imamura T., Yanase T. Hemoglobin Sawara: α6(A4) Aspartic acidAlanine. Biochim. Biophys. Acta 1973; 322: 23
   PubMed Web of Science ®Google Scholar
• Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M. Increased oxygen affinity for Hemoglobin Sawara: αA4(6) Aspartic acidAlanine. Biochim. Biophys. Acta 1977; 495: 183
   PubMed Web of Science ®Google Scholar
• Jue D. L., Johnson M. H., Patchen L. C., Moo‐Penn W. F. Hemoglobin Dunn: α6(A4) Aspartic acidAsparagine. Hemoglobin 1979; 3: 137
   PubMed Web of Science ®Google Scholar
• Pootrakul S., Kematorn B., Na‐Nakorn S., Suanpan S. A new α hemoglobin variant: Haemoglobin Anantharaj alpha 11 (A9) Lysine Glutamic acid. Biochim. Biophys. Acta 1975; 405: 161
   PubMed Web of Science ®Google Scholar
• Rosa J., Maleknia N., Vergoz D., Dunet R. Une nouvelle hemo‐globine anormale: I'hemoglobin J a Paris 12 AlaAsp. Nouv. Rev. Fr. d'Hematol 1965; 6: A23
   Google Scholar
• Trincao C., Martins De Melo J., Lorkin P. A., Lehmann H. Haemoglobin J Paris in the South of Portugal (Algarve). Acta Haematol 1968; 39: 291
   PubMed Web of Science ®Google Scholar
• Marti H. R., Pik C., Mosimann P. Eine neue hamoglobin I vari‐ante: Hb I Interlaken. Acta Haematol 1964; 32: 9
   PubMed Web of Science ®Google Scholar
• Liddell J., Brown D., Beale D., Lehmann H., Huntsman R. G. A new haemoglobin ‐ J Oxford found during a survey of an English population. Nature 1964; 204: 269
   PubMed Web of Science ®Google Scholar
• Silvestroni E., Bianco I., Tentori L., Vivaldi G., Carta S., Sorcini M., Brancati C. (1967) The structural abnormality of Hemoglobin N present in a family from Cosenza. Proc. 10th Congr. Eur. Soc. Hematol. Part II, Strasbourg, 1965. Karger, Basel/New York, 232
   Google Scholar
• Vella F., Casey R., Lehmann H., Labossiere A., Jones T. G. Haemoglobin Ottawa: α2 15 (A13) GlyArg β2. Biochim. Biophys. Acta 1974; 336: 25
   Web of Science ®Google Scholar
• Pootrakul S., Srichiyanont S., Wasi P., Suanpan S. Hemoglobin Siam α2 15 Arg β2): A new α chain variant. Humangenetik 1974; 23: 199
   PubMedGoogle Scholar
• Beale D., Lehmann H. Abnormal haemoglobins and the genetic code. Nature 1965; 207: 259
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Alperin J. B., Beale D., Lehmann H. Hemoglobin I in an American Negro family: Structural and hematologic studies. J. Lab. Clin. Med 1966; 68: 940
   PubMed Web of Science ®Google Scholar
• Bowman B. H., Barnett D. R. Amino‐acid substitution in Haemoglobin I (Texas variant). Nature 1967; 214: 499
   PubMed Web of Science ®Google Scholar
• O'Brien C., Gray M. J., Jacobs A. S. A survey of cord blood for abnormal hemoglobin with further observations on Hemoglobin I Burlington. Am. J. Obstet. Gynecol 1964; 88: 816
   PubMed Web of Science ®Google Scholar
• Baur E. W. Hb α2 glu β2 (Hb I) in a Caucasian family: Independent mutation or common origin?. Humangenetik 1968; 6: 368
   PubMedGoogle Scholar
• Griffiths K. D., Lang A., Lehmann H., Mann J. R., Plowman D., Raine D. N. Haemoglobin Handsworth α18 (A16) GlycineArginine. FEBS Lett 1977; 75: 93
   PubMed Web of Science ®Google Scholar
• Rahbar S., Ala F., Akhavan E., Nowzari G., Shoa'i I., Zamanian‐poor M. H. Two new haemoglobins: Haemoglobin Perspolis ‘α64 (E13) AspTyr’ and Haemoglobin J‐Kurosh ‘α19 (AB1) AlaAsp’. Biochim. Biophys. Acta 1976; 427: 119
   PubMed Web of Science ®Google Scholar
• Kendall A. G., Barr R. D., Lang A., Lehmann H. Haemoglobin J Nyanza: α21 (B2) AlaAsp. Biochim. Biophys. Acta 1973; 310: 357
   PubMed Web of Science ®Google Scholar
• Gottlieb A. J., Restrepo A., Itano H. A. Hemoglobin J Medellin. Chemical and genetic study. Fed. Proc 1964; 23: 172
   Google Scholar
• Kraus A. P., Miyaji T., Iuchi I., Kraus L. M. Memphis. A new variety of sickle cell anemia with clinically mild symptoms due to an α‐chain variant of hemoglobin α23 Glu NH2). J. Lab. Clin. Med 1965; 66: 886
   Web of Science ®Google Scholar
• Boyer S. H., Crosby E. F., Fuller G. F., Ulenurm L., Buck A. A. A survey of hemoglobins in the Republic of Chad and characterization of Hemoglobin Chad. α2 23 GluLys β2. Am. J. Hum. Genet 1968; 20: 570
   PubMed Web of Science ®Google Scholar
• Marengo‐Rowe A. J., Beale D., Lehmann H. New human hae‐mo‐globin variant from southern Arabia: G‐Audhali (α23 (B4) Glutamic acidValine) and the variability of B4 in human haemoglobin. Nature 1968; 219: 1164
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Brimhall B., Jones R. T., Bryant R., Mitchell C. B., Goldberg A. I. Hb Fort Worth: α27 GluGly (B8) a variant present in unusually low concentration. Biochim. Biophys. Acta 1971; 243: 164
   PubMed Web of Science ®Google Scholar
• Ahern E., Ahern V., Holder W., Palomino E., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin Spanish Town α27 GluVal (B8). Biochim. Biophys. Acta 1976; 427: 530
   PubMed Web of Science ®Google Scholar
• Vettore L., DeSandre G., Dilorio E. E., Winterhalter K. H., Lang A., Lehmann H. A new abnormal hemoglobin O Padova, α30 (B11) GluLys and a dyserythropoietic anemia with erythroblastic multinuclearity co‐existing in the same patient. Blood 1974; 44: 869
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Jim R. T. S. A new haemoglobin variant (the ‘Honolulu Type’) in a Chinese. Nature 1961; 190: 454
   PubMed Web of Science ®Google Scholar
• Vella F., Ager J. A. M., Lehmann H. An abnormal haemoglobin in a Chinese: Haemoglobin G. Nature 1958; 182: 460
   PubMed Web of Science ®Google Scholar
• Swenson R. T., Hill R. L., Lehmann H., Jim R. T. S. A chemical abnormality in Hemoglobin G from Chinese individuals. J. Biol. Chem 1962; 237: 1517
   Web of Science ®Google Scholar
• Marinucci M., Mavilio F., Tentori L., D'Erasmo F., Colapietro A., De Stasio G., Di Fonzo S. A new human hemoglobin variant: Hb Bari (α 45(CD3) HisGln β2). Biochim. Biophys. Acta 1980; 622: 315
   PubMed Web of Science ®Google Scholar
• Beretta A., Prato V., Gallo E., Lehmann H. Haemoglobin Torino ‐ α43 (CD1) PhenylalanineValine. Nature 1968; 217: 1016
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsouka M., Yokoyama M., Numakura H., Nagata K., Takebe Y., Izumi Y., Shibata S. Hemoglobin Hirosaki (α43 ‘CE1’ PheLeu), a new unstable variant. Biochim. Biophys. Acta 1975; 405: 155
   PubMed Web of Science ®Google Scholar
• Braconnier F., Gacon G., Thillet J., Wajcman H., Soria J., Maigret P., Labie D., Rosa J. Hemoglobin Fort de France α245 (CD3) HisArg β2) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1977; 493: 228
   PubMed Web of Science ®Google Scholar
• Sumida I. Studies of abnormal hemoglobins in Western Japan. Frequency of visible hemoglobin variants, and chemical characterization of Hemoglobin Sawara (α26Alaβ2) and Hemoglobin Mugino (Hb L Ferrara; α247Glyβ2). Jap. J. Hum. Genet 1975; 19: 343
   Google Scholar
• Fujimura T., Kawasaki K., Imamura T., Ohta Y., Hanada M., Yamaoka K. Two kindreds of abnormal hemoglobins: Hb Tagawa I and Hb Tagawa II. Jap. J. Clin. Hematol 1964; 6: 71
   Google Scholar
• DeVries A., Joshua H., Lehmann H., Hill R. L., Fellows R. E. The first observation of an abnormal haemoglobin in a Jewish family: Haemoglobin Beilinson. Br. J. Haematol 1963; 9: 484
   PubMed Web of Science ®Google Scholar
• Halbrecht I., Isaacs W. A., Lehmann H., Ben‐Porat F. Hemoglobin Hasharon (α47 Aspartic acidHistidine). Israel J. Med. Sci 1967; 3: 827
   PubMedGoogle Scholar
• Ostertag W., Smith E. W. Hb Sinai: A new α chain mutant α47 His. Humangenetik 1968; 6: 377
   PubMedGoogle Scholar
• Schneider R. G., Ueda S., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sealy (α2 47His β2): A new variant in a Jewish family. Am. J. Hum. Genet 1968; 20: 151
   PubMed Web of Science ®Google Scholar
• Bianco I., Modiano G., Bottini E., Lucci R. Alteration in the α‐chain of Haemoglobin L Ferrara. Nature 1963; 198: 395
   PubMed Web of Science ®Google Scholar
• Tentori L. Hemoglobin L Ferrara = Hemoglobin Hasharon. Hemoglobin 1977; 1: 602
   Google Scholar
• Rahbar S., Mahdavi N., Nowzari G., Mostafavi I. Hemoglobin Arya α2 47(CD5) Aspartic acidAsparagine. Biochim. Biophys. Acta 1975; 386: 525
   PubMed Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Schneider R. G., Hosty T. S., Tomlin G., Atkins R. Two new hemoglobins: Hemoglobin Alabama β39 (C5) GlnLys) and Hemoglobin Montgomery (α48 (CD6) LeuArg). Biochim. Biophys. Acta 1975; 379: 28
   PubMed Web of Science ®Google Scholar
• Tangheroni W., Zorcolo G., Gallo E., Lehmann H. Haemoglobin J Sardegna: α50 (CD8) HistidineAspartic acid. Nature 1968; 218: 470
   PubMed Web of Science ®Google Scholar
• Cabannes R., Renaud R., Mauran A., Pennors H., Charlesworth D., Price B. G., Lehmann H. Deux hemoglobines rapides an Cote‐D'Ivoire: I'Hb K Woolwich et une nouvelle hemoglobine, I'Hb J Abidjan (α51 GlyAsp). Nouv. Rev. Fr. d'Hematol 1972; 12: 289
   PubMedGoogle Scholar
• Reynolds C. A., Huisman T. H. J. Hemoglobin Russ or α2 51 Arg β2. Biochim. Biophys. Acta 1966; 130: 541
   PubMed Web of Science ®Google Scholar
• Alberti R., Mariuzzi G. M., Artibani L., Bruni E., Tentori L. A new haemoglobin variant: J‐Rovigo alpha 53 (E‐2) AlanineAspartic acid. Biochim. Biophys. Acta 1974; 342: 1
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Takeda I., Shibata S. Hemoglobin Shimonoseki (α2 54Arg β2A), a slow‐moving hemoglobin found in a Japanese family, with special reference to its chemistry. Acta Haematol. Jap 1963; 26: 531
   PubMedGoogle Scholar
• Jones R. T., Brimhall B., Lisker R. Chemical characterization of Hemoglobin Mexico and Hemoglobin Chiapas. Biochim. Biophys. Acta 1968; 154: 488
   PubMed Web of Science ®Google Scholar
• Rosa J., Labie D., Maleknia N., Blum N. Sur quelques hemoglobines anormales nouvelles recemment isolees en France. International Symposium on Comparative Hemoglobin Structure. Thessaloniki 1966; 140
   Google Scholar
• Fessas Ph., Kaltsoya A., Loukopoulos D., Nilsson L. ‐O. On the chemical structure of Haemoglobin Uppsala. Hum. Hered 1969; 19: 152
   PubMed Web of Science ®Google Scholar
• Pootrakul S., Boonyarat D., Kematorn B., Suanpan S., Wasi P. Hemoglobin Thailand α56 (E5) LysThr’: A new abnormal human hemoglobin. Hemoglobin 1977; 1: 781
   PubMed Web of Science ®Google Scholar
• Rahbar S., Kinderlerer J. L., Lehmann H. Haemoglobin L Persian Gulf: α57 (E6) GlycineArginine. Acta Haematol 1969; 42: 169
   PubMed Web of Science ®Google Scholar
• Baglioni C. A chemical study of Hemoglobin Norfolk. J. Biol. Chem 1962; 237: 69
   PubMed Web of Science ®Google Scholar
• Imamura T. Hemoglobin Kagoshima: An example of Hemoglobin Norfolk in a Japanese family. Am. J. Hum. Genet 1966; 18: 584
   PubMed Web of Science ®Google Scholar
• Yanase T., Hanada M., Seita M., Ohya I., Ohta Y., Imamura T., Fujimura T., Kawasaki K., Yamaoka K. Molecular basis of morbidity‐From a series of studies of hemoglobinopathies in Western Japan. Jap. J. Hum. Genet 1968; 13: 40
   Google Scholar
• Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl. Acad. Sci., USA 1961; 47: 1758
   PubMed Web of Science ®Google Scholar
• Shimizu A., Hayashi A., Yamamura Y., Tsugita A., Kitayama K. The structural study on a new hemoglobin variant, Hb M Osaka. Biochim. Biophys. Acta 1965; 97: 472
   PubMed Web of Science ®Google Scholar
• Hansen H. A., Jagenburg O. R., Johansson B. G. Studies on an abnormal hemoglobin causing hereditary congenital cyanosis. Acta Paediatr 1960; 49: 503
   PubMedGoogle Scholar
• Hollan S. R., Szelenyi J. G., Lehmann H., Beale D. A Boston‐type Haemoglobin M in Hungary: Haemoglobin M Kiskunhalas. Haematologia 1967; 1: 11
   Google Scholar
• Barclay G. P. T., Charlesworth D., Lehmann H. Abnormal haemoglobin in Zambia. A new Haemoglobin Zambia α60 (E9) LysineAsparagine. Br. Med. J 1969; 4: 595
   PubMed Web of Science ®Google Scholar
• Brimhall B., Duerst M., Hollan S. R., Stenzel P., Szelenyi J., Jones R. T. Structural characterizations of Hemoglobins J Buda (α61 (E10) LysAsn) and G Pest (α74 (EF3) AspAsn). Biochim. Biophys. Acta 1974; 336: 344
   Web of Science ®Google Scholar
• Thillet J., Blouquit Y., Perrone F., Rosa J. Hemoglobin Pontoise α63 AlaAsp (E12). A new fast moving variant. Biochim. Biophys. Acta 1977; 491: 16
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T. S., Tan T. G. H., Weng M. ‐L., Liu C. ‐S., Wang C. ‐L. Hemoglobin G Waimanalo: α64 AspAsn. Biochim. Biophys. Acta 1973; 322: 27
   PubMed Web of Science ®Google Scholar
• Ramot B., Kinderlerer J. B., Lehmann H. Geneva 1972, Cited in WHO Technical Report Series No. 509, Annex 1
   Google Scholar
• Sukumaran P. K., Merchant S. M., Desai M. P., Wiltshire B. G., Lehmann H. Haemoglobin Q India (α64(E13) Aspartic acidHistidine) associated with β‐thalassemia observed in three Sindhi families. J. Med. Genet 1972; 9: 436
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Yamamoto K., Ohba Y., Shibata S. Amino acid substitution of Hemoglobin Ube 2 (α2 68 Asp β2): An example of successful application of partial hydrolysis of peptide with 5% acetic acid. Clin. Chim. Acta 1967; 16: 347
   PubMed Web of Science ®Google Scholar
• Baglioni C., Ingram V. M. Abnormal human haemoglobins. V. Chemical investigation of Haemoglobins A, G, C, X from one individual. Biochim. Biophys. Acta 1961; 48: 253
   PubMed Web of Science ®Google Scholar
• Chernoff A. I., Pettit N., Jr. The amino acid composition of hemoglobin. VI. Separation of the tryptic peptides of Hemoglobin Knoxville No. 1 on Dowex‐1 X‐2 and Sephadex. Biochim. Biophys. Acta 1965; 97: 47
   PubMed Web of Science ®Google Scholar
• Bowman B., Barnett D. R., Hodgkinson K. T., Schneider R. G. Chemical characterization of Haemoglobin G St‐1. Nature 1966; 211: 1305
   PubMed Web of Science ®Google Scholar
• Minnich V., Cordonnier J. K., Williams W. J., Moore C. V. Alpha, beta and gamma hemoglobin polypeptide chains during the neonatal period with description of a fetal form of Hemoglobin D St. Louis. Blood 1962; 19: 137
   PubMed Web of Science ®Google Scholar
• Dance N., Huehns E. R., Shooter E. M. The chemical Investigation of Haemoglobin G Bristol and G Bristol/C. Biochim. Biophys. Acta 1964; 86: 144
   PubMed Web of Science ®Google Scholar
• Colombo B., Vidal H., Kamuzora H., Lehmann H. A new Haemoglobin J‐Habana α71 (E20) AlanineGlutamic acid. Biochim. Biophys. Acta 1974; 351: 1
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Daneshmand P. Hemoglobin Daneshgah Tehran α2 72 (EF1) HistidineArginine β2A. Nature New Biol 1973; 245: 268
   PubMedGoogle Scholar
• Pootrakul S., Dixon G. H. Hemoglobin Mahidol: A new hemoglobin α‐chain mutant. Can. J. Biochem 1970; 48: 1066
   PubMedGoogle Scholar
• Blackwell R. Q., Liu C. ‐S. Hemoglobin G Taichung: α74 AspHis. Biochim. Biophys. Acta 1970; 200: 70
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Charlesworth D., Lehmann H., Rahbar S., Tuchinda S., Lie‐lnjo L. E. Two Haemoglobins Q, α74 (EF3) and α75 (EF4) Aspartic acidHistidine. Br. J. Haematol 1970; 19: 117
   PubMed Web of Science ®Google Scholar
• Orringer E. P., Wilson J. B., Huisman T. H. J. Hemoglobin Chapel Hill or α2 74 AspGly β2. FEBS Lett 1976; 65: 297
   PubMed Web of Science ®Google Scholar
• Vella F., Wiltshire B., Lehmann H., Galbraith P. Hemoglobin Winnipeg α2 75 AspTyr β2. Clin. Biochem 1973; 6: 66
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Takeda I., Fukuba Y., Shibata S., Ohkura K. Hemoglobin Matsue‐Oki: alpha 75 (EF4) Aspartic acidAsparagine. Hemoglobin 1977; 1: 383
   PubMed Web of Science ®Google Scholar
• Van Ros G., Beale D., Lehmann H. Haemoglobin Stanleyville‐Il (α78 AsparagineLysine). Br. Med. J 1968; 4: 92
   PubMed Web of Science ®Google Scholar
• Rucknagel D. L., Brandt N. J., Spencer H. H. α‐Chain mutants of human hemoglobin contributing to the genetics of the α‐chain locus. Proc. 1st Inter‐American Symposium on Hemoglobins. Caracas 1969
   Google Scholar
• Adams J. G., III, Winter W. P., Rucknagel D. L., Spencer H. H. Biosynthesis of Hemoglobin Ann Arbor: Evidence for catabolic and feedback regulation. Science 1972; 176: 1427
   PubMed Web of Science ®Google Scholar
• Honig G. R., Shamsuddin M., Tremaine L. M., Mason R. G., Vida L. N., Sarnwick R., Shahidi N. T. Hemoglobin Nigeria (α81 SerCys), a new variant having an inhibitory effect on the gelation of a sickle hemoglobin. Blood 1978; 52(Suppl. 1)113
   Google Scholar
• Winter W. P., Rucknagel D. L., Fielding J. Identification of several rare hemoglobin variants discovered in a population survey including a new variant Hb Garden State αδ2 AlaAsp. Clin. Res 1978; 26: 22A
   Google Scholar
• Crookston J. H., Farquharson H. A., Beale D., Lehmann H. Hemoglobin Etobicoke: α84 (F5) Serine replaced by Arginine. Can. J. Biochem 1969; 47: 143
   PubMedGoogle Scholar
• Huehns E. R. The unstable hemoglobins. Bull. Soc. Chem. Biol 1970; 52: 1131
   PubMedGoogle Scholar
• Lorkin P. A., Huntsman R. G., Ager J. A. M., Lehmann H., Vella F., Darbre P. D. Haemoglobin G Norfolk: α85 (F6) AspAsn. Biochim. Biophys. Acta 1975; 379: 22
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Manasse B., Thillet J., Rosa J. Haemoglobin G Norfolk α85 (F6) AspAsn. Structural characterization by sequenator analysis and functional properties of a new variant with high oxygen affinity. FEBS Lett 1975; 50: 163
   PubMed Web of Science ®Google Scholar
• Fujiwara N., Maekawa T., Matsuda G. Hemoglobin Atago (α2 85 Tyr β2) a new abnormal human hemoglobin found in Nagasaki. Int. J. Protein Res 1971; 3: 35
   PubMedGoogle Scholar
• Reed R. E., Winter W. P., Rucknagel D. L. Haemoglobin Inkster (α2 85 Aspartic acidValine β2) coexisting with β‐thalassemia in a Caucasian family. Br. J. Haematol 1974; 26: 475
   PubMed Web of Science ®Google Scholar
• Knuth A., Pribilla W., Marti H. R., Winterhalter K. H. Hemoglobin Moabit: Alpha 86 (F7) LeuArg. A new unstable abnormal hemoglobin. Acta Haematol 1979; 61: 121
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Shibata S., Takeda I., Tamura A. Possible amino acid substitution in the α‐chain (α87 Tyr) of Hb M Iwate. Acta Haematol. Jap 1963; 26: 538
   PubMedGoogle Scholar
• Heller P., Weinstein H. G., Yakulis V. J., Rosenthal I. M. Hemoglobin M Kankakee, a new variant of Hemoglobin M. Blood 1962; 20: 287
   PubMed Web of Science ®Google Scholar
• Pik C., Tonz O. Nature of Haemoglobin M Oldenburg. Nature 1966; 210: 1182
   PubMed Web of Science ®Google Scholar
• De Traverse P. M., Lehmann H., Coquelet M. L., Beale D., Isaacs W. A. Etude d'une hemoglobine J α non encore decrite, dans une famille Francaise. Compt. R. Sceanc. Soc. Biol 1966; 160: 2270
   PubMed Web of Science ®Google Scholar
• Vella F., Charlesworth D., Lorkin P. A., Lehmann H. Hemoglobin Broussais α90 LysAsn. Can. J. Biochem 1970; 48: 908
   PubMedGoogle Scholar
• Braconnier F., Cohen‐Solal M., Schlegel N., Blouquit Y., Thillet J., Cassius De Linval J., Rosa J. Hemoglobin J. Broussais α2 90 LysAsn β2A (FG2), decouverte dans une famille Martiniquaise. Nouv. Rev. Fr. d'Hematol 1975; 15: 333
   PubMedGoogle Scholar
• Hyde R. D., Kinderlerer J. L., Lehmann H., Hall M. D. Haemoglobin J Rajappen: α90 (FG2) LysThr. Biochim. Biophys. Acta 1971; 243: 515
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Tauro G. P., Melrose W., Carrell R. W. Haemoglobin Port Phillip α91 (FG3) LeuPro. A new unstable haemoglobin. FEBS Lett 1977; 81: 115
   PubMed Web of Science ®Google Scholar
• Botha M. C., Beale D., Isaacs W. A., Lehmann H. Haemoglobin J Cape Town α2 92 ArginineGlutamine β2. Nature 1966; 212: 792
   PubMed Web of Science ®Google Scholar
• Lines J. G., McIntosh R. Oxygen binding by Haemoglobin J Cape Town (α2 92 ArgGln). Nature 1967; 215: 297
   Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol 1966; 19: 91
   PubMed Web of Science ®Google Scholar
• Charache S., Weatherall D. J., Clegg J. B. Polycythemia associated with a hemoglobinopathy. J. Clin. Invest 1966; 45: 813
   PubMed Web of Science ®Google Scholar
• Wajcman H., Belkhodja O., Labie D. Hb Setif: G1(94) αAspTyr. A new a chain hemoglobin variant with substitution of the residue involved in α hydrogen bond between unlike subunits. FEBS Lett 1972; 27: 298
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Atkins R. J., Hosty T. S., Tomlin G., Casey R., Lehmann H., Lorkin P. A., Nagai K. Haemoglobin Titusville: α94 AspAsn, a new haemoglobin with a lowered affinity for oxygen. Biochim. Biophys. Acta 1975; 400: 365
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Shelton J. B., Shelton J. R., Powars D. Hemoglobin Sunshine Seth ‐ α(94(G1) AspHis) β2. Hemoglobin 1979; 3: 145
   PubMed Web of Science ®Google Scholar
• Huisman T. H. J., Adams H. R., Wilson J. B., Efremov G. D., Reynolds C. A., Wrightstone R. N. Hemoglobin G Georgia or α295 Leu (G‐2) β2. Biochim. Biophys. Acta 1970; 200: 578
   PubMed Web of Science ®Google Scholar
• Smith L. L., Plese C. L., Barton B. P., Charache S., Wilson J. B., Huisman T. H. J. Subunit dissociation of the abnormal Hemoglobin G Georgia (α2 95 (G2) β2) and Rampa (α2 95 Ser (G2) β2). J. Biol. Chem 1972; 247: 1433
   PubMed Web of Science ®Google Scholar
• De Jong W. W. W., Bernini L. F., Khan Meera P. Haemoglobin Rampa: α95 ProSer. Biochim. Biophys. Acta 1971; 236: 197
   PubMed Web of Science ®Google Scholar
• Wiltshire B. G., Clark K. G. A., Lorkin P. A., Lehmann H. Haemoglobin Denmark Hill α95 (G2) ProAla, a variant with unusual electrophoretic and oxygen binding properties. Biochim. Biophys. Acta 1972; 278: 459
   PubMed Web of Science ®Google Scholar
• Bannister W. H., Grech J. L., Plese C. F., Smith L. L., Barton B. P., Wilson J. B., Reynolds C. A., Huisman T. H. J. Hemoglobin St. Luke's or α2 95 Arg (G2) β2. Eur. J. Biochem 1972; 29: 301
   PubMedGoogle Scholar
• Crookston J. H., Farquharson H. A., Kinderlerer J. L., Lehmann H. Hemoglobin Manitoba: α102 (G9) Serine replaced by Arginine. Can. J. Biochem 1970; 48: 911
   PubMedGoogle Scholar
• Sanguansermsri T., Matragoon S., Changloah L., Flatz G. Hemoglobin Suan‐Dok (α2 109 (G16) LeuArg β2): An unstable variant associated with α‐thalassemia. Hemoglobin 1979; 3: 161
   PubMed Web of Science ®Google Scholar
• Charache S., Ostertag W., von Ehrenstein G. Clinical studies and physiological properties of Hopkins‐2 haemoglobin. Nature New Biol 1971; 234: 248
   PubMedGoogle Scholar
• Clegg J. B., Charache S. The structure of Hemoglobin Hopkins‐2. Hemoglobin 1978; 2: 85
   PubMed Web of Science ®Google Scholar
• Niazi G. A., Efremov G. D., Nikolov N., Hunter E., Jr., Huisman T. H. J. Hemoglobin Strumica or α 112(G19) HisArg β2. (With an addendum: Hemoglobin J Paris‐1 α 12 (A 10) AlaAsp β2 in the same population.). Biochim. Biophys. Acta 1975; 412: 181
   PubMed Web of Science ®Google Scholar
• Beksedic D., Rajevska T., Lorkin P. A., Lehmann H. Hb Serbia (α112(G19) HisArg), anew haemoglobin variant from Yugoslavia. FEBS Lett 1975; 58: 226
   PubMed Web of Science ®Google Scholar
• Gajdusek D. C., Guiart J., Kirk R. L., Carrell R. W., Irvine D., Kynoch P. A. M., Lehmann H. Haemoglobin J Tongariki (α115 AlanineAspartic acid): The first new haemoglobin variant found in a Pacific (Melanesian) population. J. Med. Genet 1967; 4: 1
   PubMedGoogle Scholar
• Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229
   PubMed Web of Science ®Google Scholar
• Lie‐lnjo L. E., Sadono. Haemoglobin O (Buginese X) in Sulawesi. Br. Med. J 1958; 1: 1461
   PubMedGoogle Scholar
• Sansone G., Centa A., Sciarratta V., Gallo E., Lehmann H. Haemoglobin O Indonesia (α116 GluLys) in an Italian family. Acta Haematol 1970; 43: 40
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Morito M., Iuchi I. Characterization of Hb Ube‐4: Alpha 116 (GH4) GluAla. Hemoglobin 1978; 2: 181
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Wong H. B., Wang C. ‐L., Weng M. ‐L., Liu C. ‐S. Hemoglobin J Meerut: α120 AlaGlu. Biochim. Biophys. Acta 1974; 351: 7
   PubMed Web of Science ®Google Scholar
• Kamuzora H., Lehmann H., Griffiths K. D., Mann J. R., Raine D. N. A new haemoglobin variant Hemoglobin J Birmingham α120 (H3) AlaGlu. Ann. Clin. Biochem 1974; 11: 53
   Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. L., Johnson M. H., Wilson S. M., Therrel B., Jr., Schmidt R. M. Hemoglobin Tarrant: α126 (H9) AspAsn. A new hemoglobin variant in the α1β1, contact region showing high oxygen affinity and reduced cooperativity. Biochim. Biophys. Acta 1977; 490: 443
   PubMed Web of Science ®Google Scholar
• Vella F., Galbraith P., Wilson J. B., Wong S. C., Folger G. C., Huisman T. H. J. Hemoglobin St. Claude or α2 127 (H10) LysThr β2. Biochim. Biophys. Acta 1974; 365: 318
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Bechtel K. C., Johnson M. H., Jue D. L., Holland S., Huff C., Schmidt R. M. Hemoglobin Jackson, α127 (H10) LysAsn. Am. J. Clin. Pathol 1976; 66: 453
   PubMed Web of Science ®Google Scholar
• Kleihauer E. F., Reynolds C. A., Dozy A. M., Wilson J. B., Moores R. R., Berenson M. P., Wright C. ‐S., Huisman T. H. J. Hemoglobin Bibba or α2 136 Pro β2, an unstable α‐chaln abnormal hemoglobin. Biochim. Biophys. Acta 1968; 154: 220
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Wong H. B., Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 222: 379
   PubMed Web of Science ®Google Scholar
• Poyart C., Krishnamoorthy R., Bursaux E., Gacon G., Labie D. Structural and functional studies of Haemoglobin Suresnes or α 141 (HC3) ArgHis β2, a new high oxygen affinity mutant. FEBS Lett 1976; 69: 103
   PubMed Web of Science ®Google Scholar
• Saenz G. F., Elizondo J., Alvarado M. A., Atmetlla F., Arrays G., Martinez G., Lima F., Colombo B. Chemical characterization of a new haemoglobin variant Haemoglobin J Cubujuqui (α 141 (HC3) ArgSer β2). Biochim. Biophys. Acta 1977; 494: 48
   PubMed Web of Science ®Google Scholar
• Mavilio F., Marinucci M., Tentori L., Fontanarosa P. P., Rossi U., Biagiotti S. Hemoglobin Legnano (α2 141 (HC3) ArgLeu β2): A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1978; 2: 249
   PubMed Web of Science ®Google Scholar
• Martinez G., Lima F., Residenti C., Colombo B. Hb J Camagüey α2 141 (HC3) ArgGly β2. A new abnormal human hemoglobin. Hemoglobin 1978; 2: 47
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Bechtel K. C., Schmidt R. M., Johnson M. H., Jue D. L., Schmidt D. E., Jr., Dunlap W. M., Opella S. J., Bonaventura J., Bonaventura C. Hemoglobin Raleigh (β11 ValineAcetylalanine). Structural and functional characterization. Biochemistry 1977; 16: 4872
   PubMed Web of Science ®Google Scholar
• Labossiere A., Vella F., Hiebert J., Galbraith P. Hemoglobin Deer Lodge: α2β2 HisArg. Clin. Biochem 1972; 5: 46
   PubMed Web of Science ®Google Scholar
• Ingram V. M. Abnormal human haemoglobins. III. The chemical difference between normal and sickle cell haemoglobins. Biochim. Biophys. Acta 1959; 36: 402
   PubMed Web of Science ®Google Scholar
• Hunt J. A., Ingram V. M. Abnormal human haemoglobins. IV. The chemical difference between normal human haemoglobin and Haemoglobin C. Biochim. Biophys. Acta 1960; 42: 409
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Oemijati S., Pribadi W., Weng M. ‐L., Liu C. ‐S. Hemoglobin G Makassar: β6 GluAla. Biochim. Biophys. Acta 1970; 214: 396
   PubMed Web of Science ®Google Scholar
• Hill R. L., Swenson R. T., Schwartz H. C. Characterization of a chemical abnormality in Hemoglobin G. J. Biol. Chem 1960; 235: 3182
   PubMed Web of Science ®Google Scholar
• Tuchinda S., Beale D., Lehmann H. A new haemoglobin in a Thai family. A case of Haemoglobin Siriraj‐β‐thalassemia. Br. Med. J 1965; 1: 1583
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Riggs A. Polymerization of hemoglobins of mouse and man. Structural basis. Science 1967; 158: 800
   PubMed Web of Science ®Google Scholar
• Tondo C. V., Bonaventura J., Bonaventura C., Brunori M., Antonini E. Functional properties of Hemoglobin Porto Alegre (α2Aβ2 SerCys) and the reactivity of its extra cysteinyl residue. Biochim. Biophys. Acta 1974; 342: 15
   PubMed Web of Science ®Google Scholar
• Arcasoy A., Casey R., Lehmann H., Cavdar A. O., Berki A. A new Haemoglobin J from Turkey ‐ Hb Ankara (β10 (A7) AlaAsp). FEBS Lett 1974; 42: 121
   PubMed Web of Science ®Google Scholar
• Monn E., Gaffney P. J., Lehmann H. Haemoglobin Sögn (β14 Arginine). A new haemoglobin variant. Scand. J. Haematol 1968; 5: 353
   PubMedGoogle Scholar
• Beuzard Y., Basset P., Braconnier F., El Gammel H., Martin L., Oudard J. L., Thillet J. Haemoglobin Saki αβ2 14 LeuPro (A11) structure and function. Biochim. Biophys. Acta 1975; 393: 182
   PubMed Web of Science ®Google Scholar
• Milner P. F., Corley C. C., Pomeroy W. L., Wilson J. B., Gravely M., Huisman T. H. J. Thalassemia intermedia caused by heterozygosity for both (β‐thalassemia and Hemoglobin Saki (β14 (All) LeuPro). Am. J. Hematol 1976; 1: 283
   PubMed Web of Science ®Google Scholar
• Kennedy C. C., Blundel G., Lorkin P. A., Lang A., Lehmann H. Haemoglobin Belfast P15 (β12) TryptophanArginine: A new unstable haemoglobin variant. Br. Med. J 1974; 4: 324
   PubMed Web of Science ®Google Scholar
• Gacon G., Wajcman H., Labie D., Varet B., Christoforov B. A second case of Haemoglobin Belfast (β15 ‘A12’ TrpArg) observed in a French patient. Acta Haematol 1976; 55: 313
   PubMed Web of Science ®Google Scholar
• Baglioni C., Weatherall D. J. Abnormal human hemoglobins. IX. Chemistry of Hemoglobin J Baltimore. Biochim. Biophys. Acta 1963; 78: 637
   PubMed Web of Science ®Google Scholar
• Weatherall D. J. Hemoglobin J (Baltimore) coexisting in a family with Hemoglobin S. Johns Hopkins Hosp. Bull 1964; 114: 1
   PubMedGoogle Scholar
• Chernoff A. I., Perillie P. E. The amino acid composition of HGB New Haven #2 (HGB N New Haven). Biochem. Biophys. Res. Commun 1964; 16: 368
   PubMed Web of Science ®Google Scholar
• Wong S. C., Bouver N., Wilson J. B., Huisman T. H. J. Hb J Georgia = Hb J Baltimore = α2β2 16 GlyAsp. Clin. Chim. Acta 1971; 35: 521
   PubMed Web of Science ®Google Scholar
• Wade P. T., Jenkins T., Huehns E. R. Haemoglobin variant in a Bushman: Haemoglobin Dβ‐Bushmanα2β216GlyArg. Nature 1967; 216: 688
   PubMed Web of Science ®Google Scholar
• Maekawa M., Maekawa T., Fujiwara N., Tabara K., Matsuda G. Hemoglobin Nagasaki: αA2β2 17 Glu. A new abnormal human hemoglobin found in one family in Nagasaki. Int. J. Prot. Res 1970; 11: 147
   Google Scholar
• Elion J., Belkhodja O., Wajcman H., Labie D. Two variants of Hemoglobin D in the Algerian population: Hemoglobin D Ouled Rabah β19 (B1) AsnLys and Hemoglobin D Iran β22 (B4) GluGln. Biochim. Biophys. Acta 1973; 310: 360
   PubMed Web of Science ®Google Scholar
• Lam H., Wilson J. B., Harris H., Gravely M., Huisman T. H. J. Hemoglobin Alamo ‘α2β2 19 (B1) AsnAsp’. Hemoglobin 1977; 1: 703
   PubMed Web of Science ®Google Scholar
• Stamatoyannopoulos G., Nute P. E., Adamson J. W., Bellingham A. J., Funk D., Hornung S. Hemoglobin Olympia (β20 ValineMethionine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J. Clin. Invest 1973; 52: 342
   PubMed Web of Science ®Google Scholar
• Vella F., Lorkin P. A., Carrell R. W., Lehmann H. A new hemoglobin variant resembling Hemoglobin E. Hemoglobin E Saskatoon: β22 GluLys. Can. J. Biochem 1967; 45: 1385
   PubMedGoogle Scholar
• Blackwell R. Q., Yang H. J., Wang C. C. Hemoglobin G Taipei: α2α2 22 GluGly. Biochim. Biophys. Acta 1969; 175: 237
   PubMed Web of Science ®Google Scholar
• Vella F., Isaacs W. A., Lehmann H. Hemoglobin G Saskatoon: β22 GluAIa. Can. J. Biochem 1967; 45: 351
   PubMedGoogle Scholar
• Blackwell R. Q., Liu C. S., Yang H. J., Wang C. C., Huang J. T. H. Hemoglobin variant common to Chinese and North American Indians: αβ2 22 GluAla. Science 1968; 161: 381
   PubMed Web of Science ®Google Scholar
• Bowman B. H., Barnett D. R., Hite R. Hemoglobin G Coushatta: a beta variant with a delta‐like substitution. Biochem. Biophys. Res. Commun 1967; 26: 466
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Ro I. H., Liu C. S., Yang H. J., Wang C. C., Huang J. T. H. Hemoglobin variant found in Koreans, Chinese, and North American Indians. α2β2 22 GluAIa. Am. J. Phys. Anthropol 1969; 30: 389
   PubMedGoogle Scholar
• Rahbar S. Haemoglobin D Iran: β22 Glutamic acidGlutamine (B4). Br. J. Haematol 1973; 24: 31
   PubMed Web of Science ®Google Scholar
• Garel M. C., Blouquit Y., Arous N., Rosa J. Hb Strasbourg αβ2 20 (B2) ValAsp: A variant at the same locus as Hb Olympia β20 ValMet. FEBS Lett 1976; 72: 1
   PubMed Web of Science ®Google Scholar
• Forget B. G. Nucleotide sequence of human β globin messenger RNA. Hemoglobin 1977; 1: 879
   PubMed Web of Science ®Google Scholar
• Ranney H. M., Jacobs A. S., Udem L., Zalusky R. Hemoglobin Riverdale‐Bronx, an unstable hemoglobin resulting from the substitution of arginine for glycine at helical residue B6 of the β polypeptide chain. Biochim. Biophys. Acta 1968; 33: 1004
   Google Scholar
• Huisman T. H. J., Brown A. K., Efremov G. D., Wilson J. B., Reynolds C. A., Uy R., Smith L. L. Hemoglobin Savannah (B6(24) β‐glycinevaline): An unstable variant causing anemia with inclusion bodies. J. Clin. Invest 1971; 50: 650
   PubMed Web of Science ®Google Scholar
• Idelson L. I., Didkowsky N. A., Casey R., Lorkin P. A., Lehmann H. New unstable haemoglobin (Hb Moscva, β24 (B6) GlyAsp) found in the U. S. S. R. Nature 1974; 249: 768
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S. Hemoglobin G Taiwan‐Ami αβ2 25 GlyArg. Biochem. Biophys. Res. Commun 1968; 30: 690
   PubMed Web of Science ®Google Scholar
• Hunt J. A., Ingram V. M. Abnormal human haemoglobins. VI. The chemical difference between Haemoglobins A and E. Biochim. Biophys. Acta 1961; 49: 520
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Arous N., Machado P. E. A., Garel M. C. Hb Henri Mondor: β26 (B8) GluVal: A varant with a substitution localized at the same position as that of Hb E β26 GluLys. FEBS Lett 1976; 72: 5
   PubMed Web of Science ®Google Scholar
• Idelson L. I., Didkowsky N. A., Filippova A. V., Casey R., Kynoch P. A. M., Lehmann H. Haemoglobin Volga, β27 (B9) AlaAsp, a new highly unstable haemoglobin with a suppressed charge. FEBS Lett 1975; 58: 122
   PubMed Web of Science ®Google Scholar
• Kuis‐Reerink J. D., Jonxis J. H. P., Niazi G. A., Wilson J. B., Bolch K. C., Gravely M., Huisman T. H. J. Hb Volga or α2β2 27 (B9) AlaAsp: An unstable hemoglobin variant in three generations of a Dutch family. Biochim. Biophys. Acta 1976; 439: 63
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Seligmann M., Thillet J., Rosa J. Haemoglobin Saint Louis β28 (B10) LeucineGlutamine. A new unstable haemoglobin only present in a ferri form. Abstract 408, XIV Intl. Cong. Hematol., Sao Paulo, 1972. FEBS Lett 1973; 33: 37
   PubMed Web of Science ®Google Scholar
• Thillet J., Cohen‐Solal M., Seligmann M., Rosa J. Functional and physicochemical studies of Hemoglobin St.: Louis β28 (B10) LeuGln. J. Clin. Invest 1976; 58: 1098
   PubMed Web of Science ®Google Scholar
• Sansone G., Carrell R. W., Lehmann H. Haemoglobin Genova: β28 (B10) LeucineProline. Nature 1967; 214: 877
   PubMed Web of Science ®Google Scholar
• Schmidt R. M., Bechtel K. C., Johnson M. H., Thrrell B. J., Jr., Moo‐Penn W. F. Hemoglobin Lufkin: β29 (B11) GlyAsp: An unstable hemoglobin variant involving an internal amino acid residue. Hemoglobin 1977; 1: 799
   PubMed Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Baur E. W., Motulsky A. G. Structural characterization of Hemoglobin Tacoma. Biochemistry 1969; 8: 2125
   PubMed Web of Science ®Google Scholar
• Jackson J. M., Yates A., Huehns E. R. Haemoglobin Perth: β32 (B14) LeuPro. An unstable haemoglobin causing haemolysis. Br. J. Haematol 1973; 25: 607
   PubMed Web of Science ®Google Scholar
• Honig G. R., Green D., Shamsuddin M., Vida L. N., Mason R. G., Gnarra D. J., Maurer H. S. Hemoglobin Abraham Lincoln, β32 (B14) LeucineProline. An unstable variant producing severe hemolytic disease. J. Clin. Invest 1973; 52: 1746
   PubMed Web of Science ®Google Scholar
• Garel M. C., Blouquit Y., Rosa J. Hemoglobin Castilla β32 (B14) LeuArg: A new unstable variant producing severe hemolytic disease. FEBS Lett 1975; 58: 145
   Web of Science ®Google Scholar
• Rieder R. F., Oski F. A., Clegg J. B. Hemoglobin Philly (β35 TyrosinePhenylalanine): Studies in the molecular pathology of hemoglobin. J. Clin. Invest 1969; 48: 1627
   PubMed Web of Science ®Google Scholar
• Yamaoka K. Hemoglobin Hirose: αβ2 37 (C3) Tryptophan yielding‐Serine. Blood 1971; 38: 730
   PubMed Web of Science ®Google Scholar
• Gacon G., Belkhodja O., Wajcman H., Labie D. Structural and functional studies of Hb Rothschild β37 (C3) TrpArg. A new variant of the α1β2 contact. FEBS Lett 1977; 82: 243
   PubMed Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Schneider R. G., Hosty T. S., Tomlin G., Atkins R. Two new hemoglobins: Hemoglobin Alabama (β39 (C5) GlnLys) and Hemoglobin Montgomery (β48 (CD6) LeuArg). Biochim. Biophys. Acta 1975; 379: 28
   PubMed Web of Science ®Google Scholar
• Kendall A. G., Pas A. T., Wilson J. B., Cope N., Bolch K., Huisman T. H. J. Hb Vaasa or αβ2 (39 (C5) GlnGlu), a mildly unstable variant found in a Finnish family. Hemoglobin 1977; 1: 292
   PubMed Web of Science ®Google Scholar
• Brown W. J., Niazi G. A., Jayalakshmi M., Abraham E. C., Huisman T. H. J. Hemoglobin Athens‐Georgia, or α2β2 40 (C6) ArgLys, a hemoglobin variant with an increased oxygen affinity. Biochim. Biophys. Acta 1976; 439: 70
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Johnson M. H., Bechtel K. C., Jue D. L., Therrell B. L., Schmidt R. M. Hemoglobin Austin and Waco: Two hemoglobins with substitutions in the α1β2 contact region. Arch. Biochem. Biophys 1977; 179: 86
   PubMed Web of Science ®Google Scholar
• Burkett L. B., Sharma V. S., Pisciotta A. V., Ranney H. M., Bruckheimer S. Hemoglobin Mequon β41 (C7) PhenylalanineTyrosine. Blood 1976; 48: 645
   PubMed Web of Science ®Google Scholar
• Dacie J. V., Shinton N. K., Gaffhey P. J., Jr., Carrell R. W., Lehmann H. Haemoglobin Hammersmith (β42 (CD1) PheSer). Nature 1967; 216: 663
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Yamaguchi K., Yonemitsu H., Ishii T., Shibata S. Hemoglobin Chiba: Hb Hammersmith in a Japanese girl. Acta Haematol. Jap 1975; 38: 53
   PubMedGoogle Scholar
• Keeling M. M., Ogden L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitchens J. L., Huisman T. H. J. Hemoglobin Louisville (β42 (CD1) PheLeu): An unstable variant causing mild hemolytic anemia. J. Clin. Invest 1971; 50: 2395
   PubMed Web of Science ®Google Scholar
• Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemoglobin BucuresLti β42 (CD1) PheLeu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. Biophys. Acta 1971; 251: 1
   PubMed Web of Science ®Google Scholar
• Bowman B. H., Oliver C. P., Barnett D. R., Cunningham J. R., Schneider R. G. Chemical characterization of three Hemoglobins G. Blood 1964; 23: 193
   Web of Science ®Google Scholar
• Iuchi I., Ueda S., Hidaka K., Shibata S. Hemoglobin Hoshida (β43 (CD2) GluGln), a new hemoglobin variant discovered in Japan. Hemoglobin 1978; 2: 235
   PubMed Web of Science ®Google Scholar
• Allan N., Beale D., Irvine D., Lehmann H. Three Haemoglobins K: Woolwich, an abnormal, Cameroon and Ibadan, two unusual variants of human Haemoglobin A. Nature 1965; 208: 658
   Web of Science ®Google Scholar
• Sick K., Beale D., Irvine D., Lehmann H., Goodall P. T., MacDougall S. Haemoglobin G Copenhagan and Haemoglobin J Cambridge. Two new bt‐chain variants of Haemoglobin A. Biochim. Biophys. Acta 1967; 140: 231
   PubMed Web of Science ®Google Scholar
• Marinucci M., Mavilio F., Tentori L., Alberti R. Hemoglobin Gavello α2β2 47 (CD6) AspGly, a new hemoglobin variant from Polesine (Italy). Hemoglobin 1977; 1: 771
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Ala F. Haemoglobin Avicenna (β47 (CD6) AspAla), a new abnormal haemoglobin. Biochim. Biophys. Acta 1979; 576: 466
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Milner P., Cobb L. Hemoglobin Okaloosa (β348 (CD7) LeucineArginine). An unstable hemoglobin with decreased oxygen affinity. J. Clin. Invest 1973; 52: 2858
   PubMed Web of Science ®Google Scholar
• Labossiere A., Hill J. R., Vella F. A new βTp V hemoglobin variant: Hb Edmonton. Clin. Biochem 1971; 4: 114
   PubMed Web of Science ®Google Scholar
• Jones R. T., Koler R. D., Duerst M. L., Dhindsa D. S. Hemoglobin Willamette ‘α2β2 51 ProArg (D2)’ a new abnormal human hemoglobin. Hemoglobin 1976; 1: 45
   PubMed Web of Science ®Google Scholar
• Konotey‐Ahulu F. I. D., Kinderlerer J. L., Lehmann H., Ringelhann B. Haemoglobin Osu‐Christiansborg: A new β‐chain variant of Haemoglobin A (β52 (D3) Aspartic acidAsparagine) in combination with haemoglobin S. J. Med. Gent 1971; 8: 302
   PubMed Web of Science ®Google Scholar
• Beresford C. H., Clegg J. B., Weatherall D. J. Haemoglobin Ocho Rios (β52 (D3) Aspartic acidAlanine); a new β‐chain variant of Haemoglobin A found in combination with Haemoglobin S. J. Med. Genet 1972; 9: 151
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol 1966; 19: 91
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S. The identical structural anomalies of Hemoglobins J Meinung and J Korat. Biochem. Biophys. Res. Commun 1966; 24: 732
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Lie‐lnjo L. E., Pribadi W. Fast hemoglobin variant in Minahassan people of Sulawesi, Chinese and Thais: αβ2 56 GlyAsp. Am. J. Phys. Anthropol 1970; 32: 147
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Haydari H., Daneshmand P. Haemoglobin Hamadan α2β2 56 GlycineArginine (D7). Biochim. Biophys. Acta 1975; 379: 645
   PubMed Web of Science ®Google Scholar
• Giardina B., Brunori M., Antonini E., Tentori L. Properties of Hemoglobin G Ferrara (β57 (E1) AsnLys). Biochim. Biophys. Acta 1978; 534: 1
   PubMed Web of Science ®Google Scholar
• Marengo‐Rowe A. J., Lorkin P. A., Gallo E., Lehmann H. Haemoglobin Dhofar ‐ a new variant from Southern Arabia. Biochim. Biophys. Acta 1968; 168: 58
   PubMed Web of Science ®Google Scholar
• Boulton F. E., Huntsman R. G., Lehmann H., Lorkin P., Romero Herrera A. Myoglobin variants. Br. J. Haematol 1971; 20: 671
   Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Shih T. ‐B. Hemoglobin J Kaohsiung: β59 LysThr. Biochim. Biophys. Acta 1971; 229: 343
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T. S., Liu C. ‐S., Weng M. ‐L., Wang C. ‐L., Shih T. ‐B. Fast hemoglobin variant found in Hawaiian‐Chinese‐Caucasian family in Hawaii and a Chinese subject in Taiwan. Vox. Sang 1972; 22: 469
   PubMed Web of Science ®Google Scholar
• Wajcman H., Amegnizin K. P. E., Belkhodja O., Labie D. Hemoglobin J Lome β59 (E3) LysAsn. A new fast moving variant found in a Togolese. FEBS Lett 1977; 84: 372
   PubMed Web of Science ®Google Scholar
• Kagimoto T., Morino Y., Kishimoto S. A new hemoglobin variant Hb Yatsushiro α2Aβ2 60 ValLeu. Biochim. Biophys. Acta 1978; 532: 195
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huehns E. R., Motulsky A. G. Structural characterization of Hemoglobin N Seattle: αAβ2 61 LysGlu. Biochim. Biophys. Acta 1968; 154: 278
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Iuchi I., Ueda S., Takeda I. Hemoglobin Hikari (α2Aβ2 61 AspNH2): A fast moving hemoglobin found in two unrelated Japanese families. Clin. Chim. Acta 1964; 10: 101
   PubMed Web of Science ®Google Scholar
• Beutler E., Lang A., Lehmann H. Hemoglobin Duarte: αβ2 62 (E6) AlaPro: A new unstable hemoglobin with increased oxygen affinity. Blood 1974; 43: 527
   PubMed Web of Science ®Google Scholar
• Muller C. J., Kingma S. Haemoglobin Zürich αAβ2 63 Arg. Biochim. Biophys. Acta 1961; 50: 595
   PubMed Web of Science ®Google Scholar
• Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl Acad. Sci., USA 1961; 47: 1758
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Iuchi I., Ueda S. A comparative study of Hemoglobin M Iwate and Hemoglobin M Kurume by means of electrophoresis, chromatography and analysis of peptide chains. Acta Haematol. Jap 1961; 24: 486
   Google Scholar
• Murawski K., Szymanowska Z., Kozlowska J. A new variant of abnormal methaemoglobin: Hb M Radom. Biochim. Biophys. Acta 1963; 69: 442
   Web of Science ®Google Scholar
• Hobolth N. Haemoglobin M Arhus: I. Clinical family study. Acta Paediatr. Scand 1965; 54: 357
   Web of Science ®Google Scholar
• Josephson A. M., Weinstein H. G., Yakulis V. J., Singer L., Heller P. A new variant of Hemoglobin M disease: Hemoglobin M Chicago. J. Lab. Clin. Med 1962; 59: 918
   PubMed Web of Science ®Google Scholar
• Betke K., Groschner E., Bock K. Properties of a further variant of Haemoglobin M. Nature 1960; 188: 864
   Web of Science ®Google Scholar
• Hörlein H., Weber G. Über chronishe familiäre methämoglobinämie und eine neue modifikation des methämoglobins. Deutsche Med. Wschr 1948; 73: 476
   PubMedGoogle Scholar
• Efremov G. D., Huisman T. H. J., Stanulovic M., Zurovec M., Duma H., Wilson J. B., Jeremic V. Haemoglobin M Saskatoon and Haemoglobin M Hyde Park in two Yugoslavian families. Scand. J. Haematol 1974; 13: 48
   PubMedGoogle Scholar
• Kohne E., Grosze H. P., Versmold H., Kley H. P., Kleihauer E. Hb M Erlangen: αβ2 63 (E7) Tyr. Eine neue mutation mit hämolyse und diaphorasemangel. Z. Kinderheilk 1975; 120: 69
   PubMedGoogle Scholar
• Wajcman H., Krishnamoorthy R., Gacon G., Elion J., Allard C., Labie D. A new hemoglobin variant involving the distal histidine: Hb Bicetre (β63 (E7) HisPro). J. Mol. Med 1976; 1: 187
   Google Scholar
• Tentori L. Three examples of double heterozygosis beta‐thalassemia and rare hemoglobin variants. Intl. Symp. Abnormal Hemoglobin and Thalassemia. IstanbulTurkey 1974, Abstract 68
   Google Scholar
• Ricco G., Pich P. G., Mazza U., Rossi G., Ajmar F., Arese P., Gallo E. Hb J Sicilia: β65 (E9) LysAsn, a beta homologue of Hb Zambia. FEBS Lett 1974; 39: 200
   PubMed Web of Science ®Google Scholar
• Garel M. C., Hassan W., Coquelet M. T., Goossens M., Rosa J. Hemoglobin J Cairo: β65 (E9) LysGln, a new hemoglobin variant discovered in an Egyptian family. Biochim. Biophys. Acta 1976; 420: 97
   PubMed Web of Science ®Google Scholar
• Rosa J., Labie D., Wajcman H., Boigne J. M., Cabannes R., Bierme R., Ruffie J. Haemoglobin I Toulouse: β66 (E10) LysGlu: A new abnormal haemoglobin with a mutation localized on the E10 porphyrin surrounding zones. Nature 1969; 223: 190
   PubMed Web of Science ®Google Scholar
• Steadman J. H., Yates A., Huehns E. R. Idiopathic Heinz body anaemia: Hb‐Bristol (067 (E11) ValAsp). Br. J. Haematol 1970; 18: 435
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Lorkin P. A., Raik E., Hunter E. Haemoglobin Sydney: β67 (E11) ValineAlanine: An emerging pattern of unstable haemoglobins. Nature 1967; 215: 626
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T. Hemoglobin Mizuho or beta 68 (E12) LeucineProline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin 1977; 1: 467
   PubMed Web of Science ®Google Scholar
• Salomon H., Tatarski I., Dance N., Huehns E. R., Shooter E. M. A new hemoglobin variant found in a Beduin tribe: Hemoglobin “Rambam”. Israel J. Med. Sci 1965; 1: 836
   PubMedGoogle Scholar
• Kurachi S., Hermodson M., Hornung S., Stamatoyannopoulos G. Structure of Haemoglobin Seattle. Nature New Biol 1973; 243: 275
   PubMedGoogle Scholar
• Carrell R. W., Owen M. C. A new approach to haemoglobin variant identification. Haemoglobin Christchurch β71 (E15) PhenylalanineSerine. Biochim. Biophys. Acta 1971; 236: 507
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Pootrakul S., Gray G. Hemoglobin Vancouver ‘α2β2 73 (E17) AspTyr’: Its structure and function. J. Mol. Evol 1976; 9: 37
   PubMed Web of Science ®Google Scholar
• Konotey‐Ahulu F. I. D., Gallo E., Lehmann H., Ringelhann B. Haemoglobin Korle‐Bu (β73 Aspartic acidAsparagine) showing one of the two amino acid substitutions of Haemoglobin C Harlem. J. Med. Genet 1968; 5: 107
   PubMedGoogle Scholar
• Lehmann H., Beale D., Bio‐Doku F. S. Haemoglobin GAccra. Nature 1964; 203: 363
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Hosty T. S., Tomlin G., Atkins R., Brimhall B., Jones R. T. Hb Mobile ‘α2β2 73 (E17) AspVal’: A new variant. Biochem. Genet 1975; 13: 411
   PubMed Web of Science ®Google Scholar
• Rieder R. F., Wolf D. J., Clegg J. B., Lee S. L. Rapid postsynthetic destruction of unstable Haemoglobin Bushwick. Nature 1975; 254: 725
   PubMed Web of Science ®Google Scholar
• White J. M., Brain M. C., Lorkin P. A., Lehmann H., Smith M. Mild “unstable haemoglobin haemolytlc anaemia” caused by Haemoglobin Shepherds Bush (β74 (E18) GlyAsp). Nature 1970; 225: 939
   PubMed Web of Science ®Google Scholar
• Hubbard M., Winton E. F., Lindeman J. G., Dessauer P. L., Wilson J. B., Wrightstone R. N., Huisman T. H. J. Hemoglobin Atlanta or αβ2 75 LeuPro (E19): An unstable variant found in several members of a Caucasian family. Biochim. Biophys. Acta 1975; 386: 538
   PubMed Web of Science ®Google Scholar
• Romain P. L., Schwartz A. D., Shamsuddin M., Adams J. G., III, Mason R. G., Vida L. N., Honig G. R. Hemoglobin J‐Chicago (β76 (E20) AlaAsp): A new hemoglobin variant resulting from a substitution of an external residue. Blood 1975; 45: 387
   PubMed Web of Science ®Google Scholar
• Rahbar S., Beale D., Isaacs W. A., Lehmann H. Abnormal haemoglobins in Iran. Observation of a new variant ‐ Haemoglobin J Iran (α2β2 77 HisArg). Br. Med. J 1967; 1: 674
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Shih T. ‐B., Wang C. ‐L., Liu C. ‐S. Hemoglobin G‐Hsi‐Tsou: β79 AspGly. Biochim. Biophys. Acta 1972; 257: 49
   PubMedGoogle Scholar
• Benesch R., Edilji R., Benesch R. E. Oxygenation properties of hemoglobin variants with substitutions near the polyphosphate binding site. Biochim. Biophys. Acta 1975; 393: 368
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Yang H. T., Wang C. C. Hemoglobin G‐Szuhu: β80 AsnLys. Biochim. Biophys. Acta 1969; 188: 59
   PubMed Web of Science ®Google Scholar
• Imai K., Morimoto H., Kotani M., Shibata S., Miyaji T., Masutomo K. Studies on the function of abnormal hemoglobins. II. Oxygen equilibrium of abnormal hemoglobins: Shimonaseki, Ube II, Hikari, Gifu, and Agenogi. Biochim. Biophys. Acta 1970; 200: 197
   PubMedGoogle Scholar
• Schneider R. G., Hettig R. A., Bilunos M., Brimhall B. Hemoglobin Baylor ‘α2β2 81 (EF5) LeuArg’ ‐ an unstable mutant with high oxygen affinity. Hemoglobin 1976; 1: 85
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. L., Bechtel K. C., Johnson M. H., Schmidt R. M., McCurdy P. R., Fox J., Bonaventura J., Sullivan B., Bona‐ventura C. Hemoglobin Providence. A human hemoglobin variant occurring in two forms in vivo. J. Biol. Chem 1976; 251: 7557
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Bonaventura C., Sullivan B., Ferruzzi G., McCurdy P. R., Fox J., Moo‐Penn W. F. Hemoglobin Providence. Functional consequences of two alterations of the 2,3‐diphosphoglycerate binding site at position β82. J. Biol. Chem 1976; 251: 7563
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Stephens A. D., Beard M. E. J., Wrigley P. F. M., Adams L., Lehmann H. Haemoglobin Rahere (β82 LysThr): A new high affinity haemoglobin associated with decreased 2,3‐diphosphoglycerate binding and relative polycythaemia. Br. Med. J 1975; 4: 200
   PubMed Web of Science ®Google Scholar
• Ikkala E., Koskela J., Pikkarainen P., Rahiala E. ‐L., El‐Hazmi M. A. F., Nagal K., Lang A., Lehmann H. Hb Helsinki: A variant with a high oxygen affinity and a substitution at a 2,3‐DPG binding site (β82 ‘EF6’ LysMet). Acta Haematol 1976; 56: 257
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Wang C. ‐L. Hemoglobin Ta‐Li: β83 GlyCys. Biochim. Biophys. Acta 1971; 243: 467
   PubMed Web of Science ®Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos (α2β2 83 (EF7) GlyAsp). A new hemoglobin (Hb) variant. Abstract 168. Annual Meeting of the American Society of Hematology. Miami 1972
   Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos α2β2 83 (EF7) GlyAsp: A new hemoglobin variant in double heterozygosity with Hemoglobin. S. Blood 1976; 47: 827
   PubMed Web of Science ®Google Scholar
• Bradley T. B., Wohl R. C., Murphy S. B., Oski F. A., Bunn H. F. Properties of Hemoglobin Bryn Mawr, β85 PheSer, a new spontaneous mutation producing an unstable hemoglobin with high oxygen affinity. Abstract 40. Annual Meeting of the American Society of Hematology. Miami 1972
   Google Scholar
• de Weinstein B. I., White J. M., Wiltshire B. G., Lehmann H. A new unstable haemoglobin: Hb Buenos Aires, β85 (F1) PheSer. Acta Haematol 1973; 50: 357
   PubMed Web of Science ®Google Scholar
• Watson‐Williams E. J., Beale D., Irvine D., Lehmann H. A new haemoglobin, D Ibadan (β87 ThreonineLysine), producing no sickle cell Haemoglobin D disease with Haemoglobin S. Nature 1965; 205: 1273
   PubMed Web of Science ®Google Scholar
• Hollender A., Lorkin P. A., Lehmann H., Svensson B. New unstable Haemoglobin Boras: β88 (F4) LeucineArginine. Nature 1969; 222: 953
   PubMed Web of Science ®Google Scholar
• Opfell R. W., Lorkin P. A., Lehmann H. Hereditary nonspherocytic haemolytlc anaemia with post‐splenectomy inclusion bodies and pigmenturia caused by an unstable Haemoglobin Santa Ana ‐ β88 (F4) LeucineProline. J. Med. Genet 1968; 5: 292
   PubMedGoogle Scholar
• Thillet J., Blouquit Y., Garel M. C., Dreyfus B., Reyes F., Cohen‐Solal M., Beuzard Y., Rosa J. Hemoglobin Creteil B89 (F5) SerAsn: High oxygen affinity variant of hemoglobin frozen in a quaternary R‐structure. J. Mol. Med 1976; 1: 135
   Google Scholar
• Paniker N. V., Kuang‐Tzu Davis Lin, Krantz S. B., Flexner J. M., Wasserman B. K., Puett D. Haemoglobin Vanderbilt (α2β2 89 SerArg): A new haemoglobin with high oxygen affinity and compensatory erythrocytosis. Br. J. Haematol 1978; 39: 249
   PubMed Web of Science ®Google Scholar
• Miyaji R., Suzuki H., Ohba Y., Shibata S. Hemoglobin Agenogi (α2bt2 90 Lys), a slow moving hemoglobin of a Japanese family resembling Hb‐E. Clin. Chim. Acta 1966; 14: 624
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Satoshi U., Alperine J. B., Brimhall B., Jones R. T. Hemoglobin Sabine, β91 (F7) LeuPro. An unstable variant causing severe anemia with inclusion bodies. N. Engl. J. Med 1969; 280: 739
   PubMed Web of Science ®Google Scholar
• Ahern E., Ahern C., Hilton T., Serjeant G. R., Serjeant B. E., Seakins M., Lang A., Middleton A., Lehmann H. Haemoglobin Caribbean, β91 (F7) LeuArg: A mildly unstable haemoglobin with low oxygen affinity. FEBS Lett 1976; 69: 99
   PubMed Web of Science ®Google Scholar
• Heller P., Coleman R. D., Yakulis V. Hemoglobin M Hyde Park: A new variant of abnormal methemoglobin. J. Clin. Invest 1966; 45: 1021
   Web of Science ®Google Scholar
• Shibata S., Yamamoto K., Ohba Y., Miyaji R., Karita K., Iuchi I. Hemoglobin M Akita disease. Acta Haematol. Jap 1969; 32: 311
   Google Scholar
• Beuzard Y., Courvalin J. C. L., Cohen‐Solal M., Garel M. C., Rosa J., Brizard C. P., Gibaud A. Structural studies of Hemoglobin Saint Etienne β92 (F8) HisGln: A new abnormal hemoglobin with loss of β proximal histidine and absence of heme on the β chains. FEBS Lett 1972; 27: 76
   PubMed Web of Science ®Google Scholar
• Aksoy M., Erdem S., Efremov G. D., Wilson J. B., Huisman T. H. J., Schroeder W. A., Shelton J. R., Shelton J. B., Ulitin O. N., Muftuglu A. Hemoglobin Istanbul: Substitution of Glutamine for Histidine in a proximal Histidine (F8(92) β). J. Clin. Invest 1972; 51: 2380
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Przywara K. P., Heller P., Shamsuddin M. Hemoglobin J Altgeld Gardens: A hemoglobin variant with a substitution of the proximal histidine of the β‐chain. Hemoglobin 1978; 2: 403
   PubMed Web of Science ®Google Scholar
• Finney R., Casey R., Lehmann H., Walker W. Hb Newcastle: β92 (F8) HisPro. FEBS Lett 1975; 60: 435
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. An improved method for the characterization of human haemoglobin mutants: Identification of α2β2 95 Glu, Haemoglobin N (Baltimore). Nature 1965; 207: 945
   PubMed Web of Science ®Google Scholar
• Gottlieb A. J., Robinson E. A., Itano H. A. Primary structure of Hopkins‐I haemoblobin. Nature 1967; 214: 189
   PubMed Web of Science ®Google Scholar
• Dobbs N. B., Jr., Simmons J. W., Wilson J. B., Huisman T. H. J. Hemoglobin Jenkins or Hemoglobin N‐Baltimore or αβ2 95 Glu. Biochim. Biophys. Acta 1966; 117: 492
   PubMed Web of Science ®Google Scholar
• Bayrakci C., Josephson A., Singer L., Heller P., Coleman R. D. A new fast hemoglobin. Xth Congress of the International Society of Haematology. StockholmSweden 1964
   Google Scholar
• Hamilton H. H., Iuchi I., Miyaji T., Shibata S. Hemoglobin Hiroshima (β143 HistidineAspartic acid): A newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia. (Personal communication, P. Heller). J. Clin. Invest 1969; 48: 525
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Schneider R. G., Andrian S., Das D. K. Hemoglobin Detroit: β95 (FG2) LysineAsparagine. Biochim. Biophys. Acta 1978; 536: 283
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Lehmann H., Fairbanks V. F., Berglund G., Leonhardt T. Two new pathological haemoglobins: Olmsted β141 (H19) LeuArg and Malmö: β97 (FG4) HisGln. Biochem. J 1970; 119: 68
   Web of Science ®Google Scholar
• Taketa F., Huang Y. P., Libnoch J. A., Dessell B. H. Hemoglobin Wood β97 (FG4) HisLeu: A new high‐oxygen affinity hemoglobin associated with familial erythrocytosis. Biochim. Biophys. Acta 1975; 400: 348
   PubMed Web of Science ®Google Scholar
• Taketa F., Antholine W. E., Mauk A. G., Libnoch J. A. Nitrosylhemoglobin Wood: Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum. Biochemistry 1975; 14: 3229
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Hutchison H. E. Haemoglobin Köln β98 ValineMethionine): An unstable protein causing inclusion‐body anaemia. Nature 1966; 210: 915
   PubMed Web of Science ®Google Scholar
• Woodson R. D., Heywood J. D., Lenfant C. Oxygen transport in Hemoglobin San Francisco. Clin. Res 1970; 18: 134
   Google Scholar
• Ohba Y., Miyaji T., Shibata S. Identical substitution in Hb Ube‐1 and Hb Köln. Nature New Biol 1973; 243: 205
   PubMedGoogle Scholar
• Gordon‐Smith E. C., Dacie J. V., Blecher T. E., French E. A., Wiltshire B. G., Lehmann H. Haemoglobin Nottingham, β98 (FG5) ValGly: A new unstable haemoglobin producing severe haemolysis. Prod. Roy. Soc. Med 1973; 66: 507
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. A new unstable hemoglobin mutated in β98 ‘FG5) ValAla: Hb Djelfa. FEBS Lett 1975; 58: 238
   PubMed Web of Science ®Google Scholar
• Reed C. S., Hampson R., Gordon S., Jones R. T., Novy M. J., Brimhall B., Edwards M. J., Koler R. D. Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, Hemoglobin Kempsey. Blood 1968; 31: 623
   PubMed Web of Science ®Google Scholar
• Jones R. T., Osgood E. E., Brimhall B., Koler R. D. Hemoglobin Yakima: I. Clinical and biochemical studies. J. Clin. Invest 1967; 46: 1840
   PubMed Web of Science ®Google Scholar
• Weatherall D. J., Clegg J. B., Callender S. T., Wells R. M. G., Gale R. E., Huehns E. R., Perutz M. F., Viggiano G., Ho C. Haemoglobin Radcliffe (α2β2 99 (G1) Ala): A high oxygen‐affinity variant causing familial polycythaemia. Br. J. Haematol 1977; 35: 177
   PubMed Web of Science ®Google Scholar
• Rucknagel D. L., Glynn K. P., Smith J. R. Hemoglobin Ypsilanti characterized by increased oxygen affinity, abnormal polymerization and erythremia. Clin. Res 1967; 15: 270
   Google Scholar
• Lokich J. J., Mahoney C. W., Bunn H. F., Bruckheimer S. M., Ranney H. M. Hemoglobin Brigham (α2Aβ2 100 ProLeu). Hemoglobin variant associated with familial erythrocytosis. J. Clin. Invest 1973; 52: 2060
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Gray G. Hemoglobin British Columbia ‘α2β2 101 (G3) GluLys’: A new variant with high oxygen affinity. Hemoglobin 1976; 1: 171
   PubMed Web of Science ®Google Scholar
• Adams J. B., Winter W. P., Tausk K., Heller P. Hemoglobin Rush ‘β‐101 (G3) Glutamine’: A new unstable hemoglobin causing mild hemolytic anemia. Blood 1974; 45: 261
   Web of Science ®Google Scholar
• Mant M. J., Salkie M. L., Cope N., Appling F., Bolch K., Jayalakshmi M., Gravely M., Wilson J. B., Huisman T. H. J. Hb Alberta or α2β2 (101 (G3) GluGly), a new high‐oxygen affinity hemoglobin variant causing erythrocytosis. Hemoglobin 1976; 1: 183–77
   PubMed Web of Science ®Google Scholar
• Charache S., Jacobson R., Brimhall B., Murphy E. A., Hathaway P., Winslow R., Jones R., Rath C., Simkovich J. Hb Potomac (β101 GluAsp): Speculations on placental oxygen transport in carriers of high‐affinity hemoglobins. Blood 1978; 51: 331
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Huisman T. H. J., Smith L. L., Wilson J. B., Kitchens J. L., Wrightstone R. N., Adams H. R. Hemoglobin Richmond, a human hemoglobin which forms asymmetric hybrids with other hemoglobins. J. Biol. Chem 1969; 244: 6105
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Riggs A. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. J. Biol. Chem 1968; 243: 980
   PubMed Web of Science ®Google Scholar
• Nagel R. L., Joshua L., Johnson J., Landau L., Bookchin R. M., Harris M. B. Hemoglobin Beth Israel: A mutant causing clinically apparent cyanosis. N. Engl. J. Med 1976; 295: 125
   PubMed Web of Science ®Google Scholar
• White J. M., Szur L., Gillies I. D. S., Lorkin P. A., Lehmann H. Familial polycythaemia caused by a new haemoglobin variant. Hb Heathrow β103 (G5) PhenylalanineLeucine. Br. Med. J 1973; 3: 665
   PubMed Web of Science ®Google Scholar
• Wilkinson T., Ching Geh Chua, Carrell R. W., Robin H., Exner T., Kit Ming Lee, Kronenberg H. A new haemoglobin variant, Haemoglobin Camperdown β104 (G6) ArginineSerine. Biochim. Biophys. Acta 1975; 393: 195
   PubMed Web of Science ®Google Scholar
• Ryrie D. R., Plowman D., Lehmann H. Haemoglobin Sherwood Forest β104 (G6) ArgThr. FEBS Lett 1977; 83: 260
   PubMed Web of Science ®Google Scholar
• Hyde R. D., Hall M. D., Wiltshire B. G., Lehmann H. Haemoglobin Southampton, β106 (G8) LeuPro: An unstable variant producing severe haemolysis. Lancet 1972; ii: 1170
   Google Scholar
• Koler R. D., Jones R. T., Bigley R. H., Litt M., Lovrien E., Brooks R., Lahey M. E., Fowler R. Hemoglobin Casper: β106 (G8) LeuPro, a contemporary mutation. Am. J. Med 1973; 55: 549
   PubMed Web of Science ®Google Scholar
• Kleihauer E., Waller H. D., Benöhr H. Chr., Kohne E., Gelinsky P. Hb Tubingen. Eine neue β‐Kettenvariante (βTp 10–12) mit erhöhter Spontanoxydation. Klin. Wschr 1971; 48: 651
   Google Scholar
• Kohne E., Kley H. P., Kleihauer E., Versmold H., Benohr H. C., Braunitzer G. Structural and functional characteristics of the Hb Tubingen: β106 (G8) LeuGln. FEBS Lett 1976; 64: 443
   PubMed Web of Science ®Google Scholar
• Turner J. W., Jr., Jones R. T., Brimhall B., Du Val M. C., Koler R. D. Characterization of Hemoglobin Burke ‘β107 (G9) GlyArg’. Biochem. Genet 1976; 14: 577
   PubMed Web of Science ®Google Scholar
• Imamura T., Fujita S., Ohta Y., Hanada M., Yanese T. Hemoglobin Yoshizuka (G10(108) β AsparagineAspartic acid): A new variant with a reduced oxygen affinity from a Japanese family. J. Clin. Invest 1969; 48: 2341
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Wolff J. A., Simon G., Vacek M., Jue D. L., Johnson M. H. Hemoglobin Presbyterian: β108 (G10) AsparagineLysine. A hemoglobin variant with low oxygen affinity. FEBS Lett 1978; 92: 53
   PubMed Web of Science ®Google Scholar
• Nute P. E., Stamatoyannopoulos G., Hermodson M. A., Roth D., Hornung S. Hemoglobinopathic erythrocytosis due to a new electro‐phoretically silent variant, Hemoglobin San Diego (β109 (G11) ValMet). J. Clin. Invest 1974; 53: 320
   PubMed Web of Science ®Google Scholar
• King M. A. R., Wiltshire B. G., Lehmann H., Morimoto H. An unstable haemoglobin with reduced oxygen affinity: Haemoglobin Peterborough, β111 (G13) ValinePhenylalanine, its interaction with normal haemoglobin and with Haemoglobin Lepore. Br. J. Haematol 1972; 22: 125
   PubMed Web of Science ®Google Scholar
• Adams J. G., Boxer L. A., Baehner R. L., Forget B. G., Tsistrokis G. A., Steinberg M. H. Hemoglobin Indianapolis (β112 ‘G14’ Arginine): An unstable β‐chain variant producing the phenotype of severe β‐thalassemia. J. Clin. Invest 1979; 63: 931
   PubMed Web of Science ®Google Scholar
• Ranney H. M., Jacobs A. S., Nagel R. L. Haemoglobin New York. Nature 1967; 213: 876
   PubMed Web of Science ®Google Scholar
• Outeirino J., Casey R., White J. M., Lehmann H. Haemoglobin Madrid, β115 (G17) AlanineProline: An unstable variant associated with haemolytic anaemia. Acta Haematol 1974; 52: 53
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin β (α2β2 117 Arg): Structure and properties. J. Lab. Clin. Med 1969; 73: 616
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Berkman N. L., Brimhall B., Jones R. T. Hemoglobin Fannin‐Lubbock ‘α2β2 119 (GH2) GlyAsp’. A slightly unstable mutant. Biochim. Biophys. Acta 1976; 543: 478
   Web of Science ®Google Scholar
• Moo‐Penn W. F., Bechtel K. C., Johnson M. H., Jue D. L., Therrell B. L., Jr., Morrison B. Y., Schmidt R. M. Hemoglobin Fannin‐Lubbock ‘αβ119 (GH2) GlyAsp’: A new hemoglobin variant at the α1β1 contact. Biochim. Biophys. Acta 1976; 453: 472
   PubMed Web of Science ®Google Scholar
• Chen‐Marotel J., Braconnier F., Blouquit Y., Martin‐Caburi J., Kammerer J., Rosa J. Hemoglobin Bougardirey‐Mali β119 (GH2) GlyVal. An electrophoretically silent variant migrating in isoelectro‐focusing as Hb F. Hemoglobin 1979; 3: 253
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Hamilton H. B. Hemoglobin Hijiyama: A new fast‐moving hemoglobin in a Japanese family. Science 1968; 159: 204
   PubMedGoogle Scholar
• El‐Hazmi M. A. F., Lehmann H. Hemoglobin Riyadh ‘α2β2 120 (GH3) LysAsn’ ‐ a new variant found in association with a‐thalassemia and iron deficiency. Hemoglobin 1976; 1: 59
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Matsuoka M., Kudoh H., Asano M., Yamamoto K., Satoh T. Hemoglobin Karatsu: Beta 120 (GH3) LysineAsparagine. An example of Hb Riyadh in Japan. Hemoglobin 1977; 1: 461
   PubMed Web of Science ®Google Scholar
• Baglioni C. Abnormal human haemoglobins. VII. Chemical studies on Haemoglobin D. Biochim. Biophys. Acta 1962; 59: 437
   PubMed Web of Science ®Google Scholar
• Ozsoylo S. Homozygous Hemoglobin D Punjab. Acta Haematol 1970; 42: 353
   Google Scholar
• Ramot B., Rotem J., Rahbar S., Jacobs A. S., Uden L., Ranney H. M. Hemoglobin D Punjab in a Bulgarian Jewish family. Israeli. Med. Sci 1969; 5: 1066
   PubMedGoogle Scholar
• Smith E. W., Conley C. L. Sickle cell‐Hemoglobin D disease. Ann. Intern. Med 1959; 50: 94
   PubMed Web of Science ®Google Scholar
• Wasi P., Pootrakul S., Na‐Nakorn S., Beale D., Lehmann H. Haemoglobin D Los Angeles (D Punjab, αβ2 125 GluNH2) in a Thai family. Acta Haematol 1968; 39: 151
   PubMed Web of Science ®Google Scholar
• Imamura T., Riggs A. Identification of Hemoglobin Oak Ridge with Hemoglobin D Punjab (Los Angeles). Biochem. Genet 1972; 7: 127
   PubMed Web of Science ®Google Scholar
• Bowman B., Ingram V. M. Abnormal human haemoglobins. VII. The comparison of normal human Haemoglobin D Chicago. Biochim. Biophys. Acta 1961; 53: 569
   PubMed Web of Science ®Google Scholar
• Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229
   PubMed Web of Science ®Google Scholar
• Kamel K., Hoerman K., Awny A. Ethnological significance of hemoglobin αβ2 121. Lys. Am. J. Phys. Anthropol 1970; 26: 107
   Web of Science ®Google Scholar
• Efremov G. D., Duma H., Rudivic R., Rolovic Z., Wilson J. B., Huis‐man T. H. J. Hemoglobin Beograd or αβ2 121 GluVal (GH4). Biochim. Biophys. Acta 1973; 328: 81
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Wong H. B., Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 22: 379
   Web of Science ®Google Scholar
• Bursaux E., Blouquit Y., Poyart C., Rosa J., Arous N., Bonn B. Hemoglobin Ty Gard (α2Aβ2 124 (H2) ProGln): A stable high O2 affinity variant at the α1β1 contact. FEBS Lett 1978; 88: 155
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Takenaka H. Japanese haemoglobin variant. Nature 1968; 217: 89
   Web of Science ®Google Scholar
• Altay C., Altinoz N., Wilson J. B., Bolch K. C., Huisman T. H. J. Hemoglobin Hacettepe or αβ2 127 (H5) GlnGlu. Biochim. Biophys. Acta 1976; 434: 1
   PubMed Web of Science ®Google Scholar
• Martinez G., Lima F., Colombo B. Haemoglobin J Guantanamo (α2β2 128 (H6) AlaAsp). A new fast unstable haemoglobin found in a Cuban family. Biochim. Biophys. Acta 1977; 491: 1
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Yang Y. ‐J., Wang C. ‐C. Hemoglobin J Taichung: β129 AlaAsp. Biochim. Biophys. Acta 1969; 194: 1
   PubMed Web of Science ®Google Scholar
• Maniatis A., Bousios T., Nagel R. L., Balazs T., Ueda Y., Bookchin R. M., Maniatis G. M. Hemoglobin Crete (β129 AlaPro): A new high‐affinity variant interacting with βd`‐ and δβd`‐thalassemia. Blood 1979; 54: 54
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Pietschmann H., Braunsteiner H., Lehmann H. Structure of Haemoglobin Wien β130 (H8) TyrosineAspartic acid: An unstable haemoglobin variant. Acta Haematol 1974; 51: 351
   PubMed Web of Science ®Google Scholar
• Wade Cohen P. T., Yates A., Bellingham A. J., Huehns E. R. Amino acid substitution on the α1β1 intersubunit contact of Haemoglobin Camden β131 (H9) GlnGlu. Nature New Biol 1973; 243: 467
   Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Ueda S., Iuchi I., Shibata S. Hemoglobin Tokuchi: β131 GlutamineGlutamic acid, an example of Hb Camden in Japan. Acta Haematol. Jap 1975; 38: 1
   PubMedGoogle Scholar
• Brennan S. O., Arnold B., Fleming P., Carrell R. W. A new unstable haemoglobin, β134 ValGlu. Proc. N. Z. Med. J 1977; 85: 398
   Google Scholar
• Arends T., Lehmann H., Plowman D., Stathopoulou R. Hemoglobin North Shore‐Caracas β134 (H12) ValineGlutamic acid. FEBS Lett 1977; 80: 261
   PubMed Web of Science ®Google Scholar
• Marti H. R., Winterhalter K. H., Di Iorio E. E., Lorkin P. A., Lehmann H. Hb Altdorf αβ2 135 (H13) AlaPro: A new electropho‐retically silent unstable haemoglobin variant from Switzerland. FEBS Lett 1976; 63: 193
   PubMed Web of Science ®Google Scholar
• Minnich V., Hill R. J., Khuri P. D., Anderson M. E. Hemoglobin Hope: A beta chain variant. Blood 1965; 25: 830
   PubMed Web of Science ®Google Scholar
• Tentori L., Carta Sorcini M., Buccella C. Hemoglobin Abruzzo: Beta 143 (H21) HisArg. Clin. Chim. Acta 1972; 38: 258
   PubMed Web of Science ®Google Scholar
• Bromberg P. A., Alben J. O., Bare G. H., Balcerzak S. P., Jones R. T., Brimhall B., Padilla F. Hemoglobin Little Rock (β143 HisGln: (H21)). A high oxygen affinity haemoglobin variant with unique properties. Nature New Biol 1973; 243: 177
   PubMedGoogle Scholar
• Jensen M., Oski F. A., Nathan D. G., Bunn H. F. Hemoglobin Syracuse (α2β2 143 (H21) HisPro), a new high‐affinity variant detected by special electrophoretic methods. J. Clin. Invest 1975; 55: 469
   PubMed Web of Science ®Google Scholar
• Zak S. J., Brimhall B., Jones R. T., Kaplan M. E. Hemoglobin Andrew‐Minneapolis α2Aβ2 144 LysAsn: A new high‐oxygen affinity mutant human hemoglobin. Blood 1974; 44: 543
   PubMed Web of Science ®Google Scholar
• Hayashi A., Stamatoyannopoulos G., Yoshida A., Adamson J. Haemoglobin Rainier: β145 ( HC2) TyrosineCysteine and Haemoglobin Bethesda: β145 (HC2) TyrosineHistidine. Nature New Biol 1971; 230: 264
   PubMedGoogle Scholar
• Kleckner H. B., Wilson J. B., Lindeman J. G., Stevens P. D., Niazi G., Hunter E., Chen C. J., Huisman T. H. J. Hemoglobin Fort Gordon or αβ2 145 TyrAsp, a new high‐oxygen affinity hemoglobin variant. Biochim. Biophys. Acta 1975; 400: 343
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Jones R. T. Polycythemia produced by Hemoglobin Osler (β145 (HC2) TyrAsp). Johns Hopkins Med. J 1975; 136: 132
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. Structural and functional study of Hb Nancy β145 (HC2) TyrAsp: A high oxygen affinity hemoglobin. FEBS Lett 1975; 56: 39
   PubMedGoogle Scholar
• Winslow R. M., Swenberg M. ‐L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin McKees Rocks (α2β2 145 TyrTerm): A human “nonsense” mutation leading to a shortened β‐chain. J. Clin. Invest 1976; 57: 772
   PubMed Web of Science ®Google Scholar
• Imai K. Oxygen‐equilibrium characteristics of abnormal Hemoglobin Hiroshima (α2β2 143 Asp). Arch. Biochem. Biophys 1968; 127: 543
   PubMed Web of Science ®Google Scholar
• Barem G. H., Bromberg P. A., Alben J. O., Brimhall B., Jones R. T., Mintz S., Rother I. Altered C‐terminal salt bridges in Haemoglobin York cause high oxygen affinity. Nature 1976; 259: 155
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kilmartin J. V., Najman A., Labie D. Hemoglobin Cochin‐Port Royal ‐ consequences of the replacement of the β chain C‐terminal by an arginine. Biochim. Biophys. Acta 1975; 400: 354
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huehns E. R., Barnicot N. A. Hemoglobin Sphakia: A delta chain variant of Hemoglobin A2 from Crete. Science 1966; 151: 1406
   PubMed Web of Science ®Google Scholar
• Ranney H. M., Jacobs A. S., Ramot B., Bradley T. B., Jr. Hemoglobin NYU, a delta chain variant, α2δ2 12 Lys. J. Clin. Invest 1969; 48: 2057
   PubMed Web of Science ®Google Scholar
• Ball E. W., Meynell M. J., Beale D., Kynoch P., Lehmann H., Stretton A. O. W. Haemoglobin A2':α2δ2 16 GlycineArginine. Nature 1966; 209: 1217
   PubMed Web of Science ®Google Scholar
• Rieder R. F., Clegg J. B., Weiss H. J., Christy N. P., Rabinowitz R. Hemoglobin A2‐Roosevelt: α2δ2 20 ValGlu. Biochim. Biophys. Acta 1976; 439: 501
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huisman T. H. J. Structural characterization of two δ chain variants. Hemoglobin A2' (B2) and Hemoglobin Flatbush. J. Biol. Chem 1967; 242: 5141
   PubMed Web of Science ®Google Scholar
• Sharma R. S., Harding D. L., Wong S. C., Wilson J. B., Gravely M. E., Huisman T. H. J. A new δ chain variant Haemoglobin A2‐Melbourne or α2δ2 43 GluLys (CD2). Biochim. Biophys. Acta 1974; 359: 233
   PubMed Web of Science ®Google Scholar
• Alberti R., Tentori L., Marinucci M., Borghesi V. Hb A2‐Adria (δ 51 ProArg (D2)): A new δ‐chain variant found in association with β‐thalassemia. Hemoglobin 1978; 2: 171
   PubMed Web of Science ®Google Scholar
• Lie‐lnjo L. E., Pribada W., Boerma F. W., Efremov G. D., Wilson J. B., Reynolds C. A., Huisman T. H. J. Hemoglobin A2‐Indonesia or αδ2 69 (E13) GlyArg. Biochim. Biophys. Acta 1971; 229: 335
   PubMedGoogle Scholar
• Sharma R. S., Williams L., Wilson J. B., Huisman T. H. J. Hemoglobin A2‐Coburg or αδ2 116 ArgHis (G18). Biochim. Biophys. Acta 1975; 393: 379
   PubMed Web of Science ®Google Scholar
• De Jong W. W. W., Bernini L. F. Haemoglobin Babinga (δ136 GlycineAspartic acid): A new delta chain variant. Nature 1968; 219: 1360
   PubMed Web of Science ®Google Scholar
• Lie‐lnjo L. E., Kamuzora H., Lehmann H. Haemoglobin F Malaysia: α2γ2 1 (NA1) GlycineCysteine: 136 Glycine. J. Med. Genet 1974; 11: 25
   PubMedGoogle Scholar
• Jenkins G. C., Beale D., Black A. J., Huntsman G. R., Lehmann H. Haemoglobin F Texas I (α2γ2 5 GluLys): A variant of Haemoglobin F. Br. J. Haematol 1967; 13: 252
   PubMed Web of Science ®Google Scholar
• Ahem E. J., Wiltshire B. G., Lehmann H. Further characterization of Haemoglobin F. Texas I dM5 Glutamic acidLysine: γ136 Alanine. Biochim. Biophys. Acta 1972; 271: 61
   PubMed Web of Science ®Google Scholar
• Larkin I. L. M., Baker T., Lorkin P. A., Lehmann H., Black A. J., Huntsman R. G. Haemoglobin F Texas II (α2γ2 6 GluLys). The second of the Haemoglobin F Texas variants. Br. J. Haematol 1968; 14: 233
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Owen M. C., Anderson R., Berry E. Haemoglobin F Auckland G 7 AspAsn ‐ further evidence for multiple genes for the gamma chain. Biochim. Biophys. Acta 1974; 365: 323
   PubMed Web of Science ®Google Scholar
• Loukopoulos D., Kaltsoya A., Fessas Ph. On the chemical abnormality of Hb “Alexandra” a fetal hemoglobin variant. Blood 1969; 33: 114
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Smith M. B., Carrell R. W. Haemoglobin F Melbourne Gγ16 GlyArg and Haemoglobin F Carlton Gγ121 GluLys. Biochim. Biophys. Acta 1977; 490: 452
   PubMed Web of Science ®Google Scholar
• Lie‐lnjo L. E., Wiltshire B. G., Lehmann H. Structural identification of Haemoglobin F Kuala Lumpur (α2γ2 22 (B4) AspGly: (136 Ala). Biochim. Biophys. Acta 1973; 322: 224
   PubMedGoogle Scholar
• Ahern E. J., Jones R. T., Brimhall B., Gray R. H. Haemoglobin F Jamaica (α2γ2 61 LysGlu: 136 Ala). Br. J. Haematol 1970; 18: 369
   PubMed Web of Science ®Google Scholar
• Ahern E., Holder W., Ahern V., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin F Victoria Jubilee (α2Aγ2 80 AspTyr). Biochim. Biophys. Acta 1975; 393: 188
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Haggard M. E., Gustavson L. P., Brimhall B., Jones R. T. Genetic haemoglobin abnormalities in about 9000 Black and 7000 White newborns: Haemoglobin F Dickinson (Aγ97HisArg), a new variant. Br. J. Haematol 1974; 28: 515
   PubMed Web of Science ®Google Scholar
• Omura H., Miyaji T., Shibata S. Hemoglobin F Ube (108 AsnLys), a new abnormal fetal hemoglobin found in a Japanese baby. Chem. Abstr 1975; 83: 266
   Google Scholar
• Cauchi M. N., Clegg J. B., Weatherall D. J. Haemoglobin F (Malta) a new foetal haemoglobin variant with a high incidence in Maltese infants. Nature 1969; 223: 311
   PubMed Web of Science ®Google Scholar
• Sacker L. S., Beale D., Black A. J., Huntsman R. G., Lehmann H., Lorkin P. A. Haemoglobin F Hull (γ121 Glutamic acidLysine), homologous with Haemoglobins O and O Indonesia. Br. Med. J 1967; 3: 531
   PubMed Web of Science ®Google Scholar
• Brimhall B., Vedvick T. S., Jones R. T., Ahern E., Palomino E., Ahem V. Haemoglobin F Port Royal (α2Gγ2 125 Glu Ala). Br. J. Haematol 1973; 27: 313
   Web of Science ®Google Scholar
• Lee‐Potter J. P., Deacon‐Smith R. A., Simpkiss M. J., Kamuzora H., Lehmann H. A new cause of haemolytic anemia in the newborn. A description of an unstable fetal haemoglobin: F Poole, αGγ2 130 TryptophanGlycine. J. Clin. Pathol 1975; 28: 317
   PubMed Web of Science ®Google Scholar
• Barnabas J., Muller C. J. Haemoglobin Lepore Hollandia. Nature 1962; 194: 931
   Google Scholar
• Ostertag W., Smith E. W. Hemoglobin‐Lepore Baltimore, a third type of a δβ crossover (δ50, p86). Eur. J. Biochem 1969; 10: 371
   PubMedGoogle Scholar
• Baglioni C. The fusion of two peptide chains in Hemoglobin Lepore and its interpretation as a genetic deletion. Proc. Natl. Acad. Sci., USA 1962; 48: 1880
   PubMed Web of Science ®Google Scholar
• Ohta Y., Yamaoka K., Sumida I., Yanase T. Hemoglobin Miyada, a β‐δ fusion peptide (anti‐Lepore) type discovered in a Japanese family. Nature New Biol 1971; 234: 218
   PubMedGoogle Scholar
• Lehmann H., Charlesworth D. Observation on Haemoglobin β (Congo type). Biochem. J 1970; 119: 43
   PubMed Web of Science ®Google Scholar
• Badr F. M., Lorkin P. A., Lehmann H. Haemoglobin P‐Nilotic: containing a β‐δ chain. Nature New Biol 1973; 242: 107
   PubMedGoogle Scholar
• Huisman T. H. J., Wrightstone R. N., Wilson J. B., Schroeder W. A., Kendall A. G. Hemoglobin Kenya, the product of fusion of γ and β polypeptide chains. Arch. Biochem. Biophys 1972; 153: 850
   PubMed Web of Science ®Google Scholar
• Milner P. F., Clegg J. B., Weatherall D. J. Haemoglobin H disease due to a unique hemoglobin variant with an elongated α‐chain. Lancet 1971; i: 729
   Google Scholar
• Weatherall D. J., Clegg J. B. The α‐chain‐termination mutants and their relation to the α‐thalassemias. Phil. Trans. Roy. Soc 1975; B127: 411
   Google Scholar
• Clegg J. B., Weatherall D. J., Contopolou‐Griva I., Caroutsos K., Poungouras P., Tsevrenis H. Haemoglobin Icaria, a new chain‐termination mutant which causes a thalassemia. Nature 1974; 251: 245
   PubMed Web of Science ®Google Scholar
• De Jong W. W. W., Khan Meera P., Bernini L. F. Hemoglobin Koya Dora: High frequency of a chain termination mutant. Am. J. Hum. Genet 1975; 27: 81
   PubMed Web of Science ®Google Scholar
• Flatz G., Kinderlerer J. L., Kilmartin J. V., Lehmann H. Haemoglobin Tak: A variant with additional residues at the end of the β‐chains. Lancet 1971; i: 732
   Google Scholar
• Imai K., Lehmann H. The oxygen affinity of Haemoglobin Tak, a variant with an elongated β chain. Biochim. Biophys. Acta 1975; 412: 288
   Web of Science ®Google Scholar
• Lehmann H., Casey R., Lang A., Stathopoulou R., Imai K., Chinda S., Vinai P., Flatz G. Haemoglobin Tak: A β‐chain elongation. Br. J. Haematol 1975; 31: 119, (Suppl.)
   Google Scholar
• Seid‐Akhaven M., Winter W. P., Abramson R. K., Rucknagel D. L. Hemoglobin Wayne: A frameshift mutation detected in human hemoglobin alpha chains. Proc. Natl. Acad. Sci. USA 1976; 73: 882
   PubMed Web of Science ®Google Scholar
• Bunn H. F., Schmidt G. J., Haney D. N., Dluhy R. G. Hemoglobin Cranston, an unstable variant having an elongated β chain due to a nonhomologous crossover between two normal β chain genes. Proc. Natl. Acad. Sci. USA 1975; 72: 3609
   PubMed Web of Science ®Google Scholar
• Huisman T. H. J., Wilson J. B., Gravely M., Hubbard M. Hemoglobin Grady: The first example of a variant with elongated chains due to an insertion of residues. Proc. Natl. Acad. Sci. USA 1974; 71: 3270
   PubMed Web of Science ®Google Scholar
• Scott A. F., Phillips J. A., III, Young K. E., Kazazian H. H., Jr., Smith K. D., Charache S., Clegg J. B. The molecular basis of Hemoglobin Grady. Am. J. Hum. Genet 1981; 33: 129
   PubMed Web of Science ®Google Scholar
• Garel M. C., Goossens M., Oudart J. L., Blouquit Y., Thillet J., Rosa J. Hemoglobin Dakar = Hemoglobin Grady: Demonstration by a new approach to the analysis of the tryptic core region of the a chain and oxygen equilibrium properties. Biochim. Biophys. Acta 1976; 453: 459
   PubMed Web of Science ®Google Scholar
• De Jong W. W. W., Went L. N., Bernini L. F. Haemoglobin Leiden: Deletion of β6 or 7 glutamic acid. Nature 1968; 220: 788
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Blouquit Y., Garel M. C., Thillet J., Gaillard L., Creyssel R., Gibaud A., Rosa J. Haemoglobin Lyon (β17–18 (A14–15) Lys‐Val0) determination of sequenator analysis. Biochim. Biophys. Acta 1974; 351: 306
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huisman T. H. J., Kleihauer E., Betke K. Hemoglobin Freiburg: Abnormal hemoglobin due to deletion of a single amino acid residue. Science 1966; 154: 1024
   PubMed Web of Science ®Google Scholar
• Praxedes H., Lehmann H. Haemoglobin Niteroi ‐ a new unstable variant. Proc. 14th International Congress of Hematology. Sao PauloBrazil 1972
   Google Scholar
• Shibata S., Miyaji T., Ueda S., Matsuoka M., Iuchi I., Yamada K., Shinkai N. Hemoglobin Tochigi (beta 56–59 deleted). A new unstable hemoglobin discovered in a Japanese family. Proc. Jap. Acad 1970; 46: 440
   Google Scholar
• Wajcman H., Labie D., Schapira G. Two new hemoglobin variants with deletion. Hemoglobin Tours: Thr β87 (F3) deleted and Hemoglobin St. Antoine: Gly‐Leu β74–75 (E18–19) deleted. Consequences for oxygen affinity and protein stability. Biochim. Biophys. Acta 1973; 295: 495
   PubMed Web of Science ®Google Scholar
• Bradley T. B., Wohl R. C., Rieder R. F. Hemoglobin Gun Hill: Deletion of five amino acid residues and impaired heme‐globin binding. Science 1967; 157: 1581
   PubMed Web of Science ®Google Scholar
• Lutcher C. L., Huisman T. H. J. Hb‐Leslie, an unstable variant due to deletion of Gin P131, occurring in combination with βd`‐thalassemia, Hb‐S, and Hb‐C. Clin. Res 1975; 23: 278A
   Google Scholar
• Lutcher C. L., Wilson J. B., Gravely M. E., Stevens P. D., Chen C. J., Linderman J. G., Wong S. C., Miller A., Gottleib M., Huisman T. H. J. Hb Leslie, an unstable hemoglobin due to deletion of glutaminyl residue β131 (H9) occurring in association with βo‐thalassemia, Hb‐C, and Hb‐S. Blood 1976; 47: 99
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. L., Bechtel K. C., Johnson M. H., Bemis E., Brosious E., Schmidt R. M. Hemoglobin Deaconess, a new deletion mutant: β131 (H9) Glutaminedeleted. Biochem. Biophys. Res. Commun 1975; 65: 8
   PubMed Web of Science ®Google Scholar
• Casey R., Kynoch P. A. M., Lang A., Lehmann H., Nozari G., Shinton N. K. Double heterozygosity for two unstable haemoglobins: Hb Sydney (β67 ‘E11’ ValAla) and Hb Coventry (β141 ‘H19’ LeuDeleted). Br. J. Haematol 1978; 38: 195
   PubMed Web of Science ®Google Scholar
• Bookchin R. M., Nagel R. L., Ranney H. M. Structure and properties of Hemoglobin C Harlem, a human hemoglobin variant with amino acid substitutions in 2 residues of the β‐polypeptide chain. J. Biol. Chem 1967; 242: 248
   PubMed Web of Science ®Google Scholar
• Lang A., Lehmann H., McCurdy P. R., Pierce L. Identification of Haemoglobin C Georgetown. Biochim. Biophys. Acta 1972; 278: 57
   PubMed Web of Science ®Google Scholar
• Adams J. G., Heller P. Hemoglobin Arlington Park: A new hemoglobin variant with two amino acid substitutions in the β chain. Hemoglobin 1977; 1: 419
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Wong H. B., Liu C. ‐S., Weng M. ‐I. Hemoglobin J Singapore: α78 AsnAsp: α79 AlaGly. Biochim. Biophys. Acta 1972; 278: 482
   PubMed Web of Science ®Google Scholar
• Goossens M., Garel M. C., Auvinet J., Basset P., Gomes P. F., Rosa J. Hemoglobin C Ziguinchor α2Aβ2 6 (A3) GluVal β58 (E2) ProArg: The second sickling variant with amino acid substitutions in 2 residues of the β polypeptide chain. FEBS Lett 1975; 58: 149
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Schmidt R. M., Jue D. L., Bechtel K. C., Wright J. M., Home M. K., III, Haycraft C. L., Roth E. F., Nagel R. L. Hemoglobin S Travis. A sickling hemoglobin with two amino acid substitutions ‘β6 (A3) Glutamic acidValine and P142 (H20) AlanineValine’. Eur. J. Biochem 1977; 77: 561
   PubMedGoogle Scholar
• Marinucci M., Mavilio F., Massa A., Gabbianelli M., Fontanarosa P. P., Camagna A., Ignesti C., Tentori L. A new abnormal human hemoglobin: Hb Prato (α2 31 (B12) ArgSer β2). Biochem. Biophys. Acta 1979; 578: 534
   PubMed Web of Science ®Google Scholar
• Abramov A., Lehmann H., Robb L. Hb Shaare Zedek (α56 E5 LysGlu). FEBS Lett 1980; 113: 235
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Steinberg M. H., Newman M. V., Morrison W. T., Benz E. J., Jr., Iyer R. β‐Thalassemia present in cis to a new β‐chain structural variant, Hb Vicksburg ‘β75 (E19) Leu0’. Proc. Natl. Acad. Sci. USA 1981; 78: 469
   PubMed Web of Science ®Google Scholar
• Wajcman H., Elion J., Boissel J. P., Labie D., Jos J., Girot R. A silent hemoglobin variant: Hemoglobin Necker Enfants‐Malades (α20 (B1) HisTyr). Hemoglobin 1980; 4: 177
   PubMed Web of Science ®Google Scholar
• Tatsis B. Hemoglobin Queens (α34 (B15) LeuArg): A new variant at the a1P1 contact. Blood 1979; 54(Suppl. 1)61a
   Google Scholar
• Honig G. R., Vida L. N., Shamsuddin M., Mason R. G., Schlumpf H. W., Luke R. A. Hemoglobin Milledgeville (α44 (CD2) ProLeu) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1980; 626: 424
   PubMed Web of Science ®Google Scholar
• Szelenyi J. G., Horanyi M., Foldi J., Hudacsek J., Istvan L., Hollan S. R. A new hemoglobin variant in Hungary: Hb Savaria α49(CE7) SerArg. Hemoglobin 1980; 4: 27
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Matsuoka I. Hemoglobin Tottori (α59 ‘E8’ GlycineValine) a new unstable hemoglobin. Hemoglobin 1981; 5: 427
   PubMed Web of Science ®Google Scholar
• Spivak V. A., Molchanova T. P., Ermakov N. V., Tokarev Y. N., Martinez G., Szelenyi J., Horanyi M., Foldi J., Hollan S., Kazieva H., Shamov I. A. A new hemoglobin variant: Hb Dagestan α60 (E9) LysGlu. Hemoglobin 1981; 5: 133
   PubMed Web of Science ®Google Scholar
• Djoumessi S., Rousseaux J., Descamps J., Goudemand M., Dautrevaux M. Hemoglobin Lille, α2 ‘74 (EF3) AspAla’ β2. Hemoglobin 1981; 5: 475
   PubMed Web of Science ®Google Scholar
• Liang C. ‐C., Chen S. ‐S., Jia P. ‐C., Wang L. ‐F., Luo H. ‐Y., Liu G. ‐Y., Liang S., Lung G. ‐F., Yu C. ‐M., Zhuang L. ‐Z., Liang B. ‐L., Tang Z. ‐N. Hemoglobin Duan, α75 (EF4) AspAla, a new variant found in China. Hemoglobin 1981; 5: 481
   PubMed Web of Science ®Google Scholar
• Iuchi I., Shimasaki S., Hidaka K., Harano T., Ueda S., Shibata S., Mizushima J., Kubo N. Hemoglobin Mizushi (α75 ‘EF4J AspGly): A new hemoglobin variant observed in a Japanese family. Hemoglobin 1980; 4: 209
   PubMed Web of Science ®Google Scholar
• Shibata S., Ueda S., Miyaji T., Imamura T. Hemoglobinopathies in Japan. Hemoglobin 1981; 5: 509
   PubMed Web of Science ®Google Scholar
• Benesch R., Personal Communication
   Google Scholar
• Ohba Y., Miyaji T., Hattori Y., Fuyuno K., Matsuoka M. Unstable hemoglobins in Japan. Hemoglobin 1980; 4: 307
   PubMed Web of Science ®Google Scholar
• Honig G. R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschmann C. Hemoglobin Petah Tikva (α110 AlaAsp): A new unstable variant with α‐thalassemia‐like expression. Blood 1981; 57: 705
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Hightower B., Carpentieri U., Duerst M. L., Shih T. B., Jones R. T. Hemoglobin Oleander α2116 (GH4) GluGln β2’: Structural and functional characterization. Hemoglobin 1980; 6: 465
   Web of Science ®Google Scholar
• Fleming P. J., Hughes W. G., Farmilo R. K., Wyatt K., Cooper W. N. Hemoglobin Westmead α2122 (H5) HisGln β2: A new hemoglobin variant with the substitution in the α1β1, contact area. Hemoglobin 1980; 4: 39
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Iuchi I. Hemoglobin Yusa (β21 (B3) AspTyr), a new abnormal hemoglobin found in Japan. Hemoglobin 1981; 5: 121
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., McPhedran P., Bobrow S., Johnson M. H., Jue D. L., Olsen K. W. Hemoglobin Connecticut (β21 (B3) AspGly): A hemoglobin variant with low oxygen affinity. Am. J. Hematol 1981; 11: 137
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Ohba Y. Abnormal hemoglobins in Japan. Hemoglobin 1980; 4: 395
   PubMed Web of Science ®Google Scholar
• Bhouquit Y., Braconnier F., Cohen‐Solal M., Foldi J., Arous N., Ankri A., Binet J. L., Rosa J. Hemoglobin Pitie‐Salpetriere β34 (B16) ValPhe a new high oxygen affinity variant associated with familial erythrocytosis. Biochim. Biophys. Acta 1980; 624: 473
   PubMedGoogle Scholar
• Wilkinson T., Brennan S. O., Carrell R. W., Wells R. M., Como P., Kronenberg H. Hemoglobin Summer Hill β52 (D3) AspHis a new variant from Sydney, Australia. Hemoglobin 1980; 4: 185
   PubMed Web of Science ®Google Scholar
• Marinucci M., Giuliani A., Maffi D., Massa A., Giampaolo A., Mavilio F., Zannotti M., Tentori L. Hemoglobin Bologna (α2β2 61 (E5) LysMet) an abnormal human hemoglobin with low oxygen affinity. Biochim. Biophys. Acta 1981; 668: 209
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Wells R. M., Smith H., Carrell R. W. Hemoglobin Brisbane: β68 LeuHis. A new high oxygen affinity variant. Hemoglobin 1981; 5: 325
   PubMed Web of Science ®Google Scholar
• Johnson C. S., Moyes D., Schroeder W. A., Shelton J. B., Shelton J. R., Beutler E. Hemoglobin Pasadena, α2β2 75 (E19) LeuArg: Identification by high performance liquid chromatography of a new unstable variant with Increased oxygen affinity. Biochim. Biophys. Acta 1980; 623: 360
   PubMed Web of Science ®Google Scholar
• Johnson M. H., Jue D. L., Patchen L. C., Hartwig E. C., Jr., Schneider N. J., Moo‐Penn W. F. Hemoglobin Tampa: β79 (EF3) Aspartic acidTyrosine. Biochim. Biophys. Acta 1980; 623: 119
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Braconnier F., Galacteros F., Arous N., Soria J., Zittoun R., Rosa J. Hemoglobin Hotel‐Dieu β99 AspGly (G1). A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1981; 5: 19
   PubMed Web of Science ®Google Scholar
• Iuchi I., Hidaka K., Harano T., Ueda S., Shibata S., Shimasaki S., Mizushima J., Kubo N., Miyake T., Uchida T. Hemoglobin Taka‐matsu (β120 (GH3) LysGln): A new abnormal hemoglobin detected in three unrelated families in the Takamatsu area of Shikoku. Hemoglobin 1980; 4: 165
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. L., Johnson M. H., Bechtel K. C., Patchen L. C. Hemoglobin variants and methods used for their characterization during 7 years of screening at the Center for Disease Control. Hemoglobin 1980; 4: 347
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Schneider R. G., Shih T. ‐B., Jones R. T., Govinda‐rajan S., Govindarajan P. G., Patchen L. C. Hemoglobin Ohio (β142 AlaAsp): A new abnormal hemoglobin with high oxygen affinity and erythrocytosis. Blood 1980; 56: 246
   PubMed Web of Science ®Google Scholar
• Hirano M., Ohba Y., Imai K., Ino T., Morishita Y., Matsui T., Shimizu S., Sumi H., Yamamoto K., Miyaji T. Hb Toyoake: β142 (H20) AlaPro. A new unstable hemoglobin with high oxygen affinity. Blood 1981; 57: 697
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Bremner J. E., Brimhall B., Jones R. T., Shih T. ‐B. Hemoglobin Cowtown (β146 HC3 HisLeu). A mutant with high oxygen affinity and erythrocytosis. Am. J. Clin. Pathol 1979; 72: 1028
   PubMed Web of Science ®Google Scholar
• Hayashi A., Fujita T., Fujimura M., Titani K. A new abnormal fetal hemoglobin, Hb F M‐Osaka (α2γ2 63 HisTyr). Hemoglobin 1980; 4: 447
   PubMed Web of Science ®Google Scholar
• Fuyuno K., Torigoe T., Ohba Y., Matsuoka M., Miyaji T. Survey of cord blood hemoglobin in Japan and identification of two new γ chain variants. Hemoglobin 1981; 5: 139
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Morrison W. T., Steinberg M. H. Hemoglobin Parchman: double crossover within a single human gene. Science 1982; 218: 291
   PubMed Web of Science ®Google Scholar
• Honig G. R., Shamsuddin M., Mason R. G., Vida L. N. Hemoglobin Lincoln Park: A δβ fusion (anti‐Lepore) variant with an amino acid deletion in the δ chain‐derived segment. Proc. Nat. Acad. Sci. USA 1978; 75: 1475
   PubMed Web of Science ®Google Scholar
• Rahbar S., Winkler K., Louis J., Rea C., Blume K., Beutler E. Hemoglobin Great Lakes (β68 ‘E12’ LeucineHistidine): A new high‐affinity hemoglobin. Blood 1981; 58: 813
   PubMed Web of Science ®Google Scholar
• Lee‐Potter J. P., Deacon‐Smith R. A., Lehmann H., Robb L. Haemoglobin Ferndown (α6 ‘A4’ Aspartic acidValine). FEBS Lett 1981; 126: 117
   PubMed Web of Science ®Google Scholar
• Zeng Y. ‐T., Huang S. ‐Z., Liang X., Long G. ‐F., Lam H., Wilson J. B., Huisman T. H. J. Hb Wuming or α2 11 (A9) LysGln β2. Hemoglobin 1981; 5: 679
   PubMed Web of Science ®Google Scholar
• Liang C., Tao H., Lo H., Huang S., Li R., Wang B. Hemoglobin Shuangfeng (α27 (B8) GluLys): A new unstable hemoglobin variant. Hemoglobin 1981; 5: 691
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Imai K., Ohba Y., Shinohara T., Horio S., Nishioka K., Shirotani H. Hemoglobin Kawachi ‘α44 (CE2) ProArg’: A new hemoglobin variant of high oxygen affinity with amino acid substitution at α1β2 contact. Hemoglobin 1982; 6: 43
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hb Handa ‘α90 (FG2) LysMet’: Structure and biosynthesis of a new slightly higher oxygen affinity variant. Hemoglobin 1982; 6: 379
   PubMed Web of Science ®Google Scholar
• Goossens M., Lee K. Y., Liebhaber S. A., Kan Y. W. Globin structural mutant α125 LeuPro is a novel cause of α‐thalassaemia. Nature 1982; 296: 864
   PubMed Web of Science ®Google Scholar
• Djoumessi S., Rousseaux J., Dautrevaux M. Structural studies of a new hemoglobin: Hb J Lens, β13 (A10) AlaAsp. FEBS Lett 1981; 136: 145
   PubMed Web of Science ®Google Scholar
• Boissel J. P., Wajcman H., Fabritius H., Cabannes R., Labie D. Application of high‐performance liquid chromatography to abnormal hemoglobin studies. Characterization of hemoglobin D in Ivory Coast and description of a new variant Hb Cocody (beta 21 (B3) Asp leads to Asn). Biochim. Biophys. Acta 1981; 670: 203
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., Shinohara T., Hori T., Takayama J. Hemoglobin Miyashiro (β23 ‘B5’ ValGly) an electrophoretically silent variant discovered by the isopropanol test. Hemoglobin 1981; 5: 653
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., Matsumoto N. A new unstable hemoglobin, Hb Yokohama β31 (B13) LeuPro, causing hemolytic anemia. Hemoglobin 1981; 5: 667
   PubMed Web of Science ®Google Scholar
• Yeager A. M., Zinkham W. H., Jue D. L., Winslow R. M., Johnson M. H., McGuffey J. E., Moo‐Penn W. F. Hemoglobin Cheverly: An unstable hemoglobin associated with mild anemia. Pediatr. Res 1983; 17: 503
   PubMed Web of Science ®Google Scholar
• Spivak V. A., Molchanova T. P., Postnikov Yu. V., Aseeva E. A., Lutsenko I. N., Tokarev Yu. N. A new abnormal hemoglobin: Hb Mozhaisk β92 (F8) HisArg. Hemoglobin 1982; 6: 169
   PubMed Web of Science ®Google Scholar
• Wajcman H., Aguilar J. L., Bascompte I., Labie D., Poyart C., Bohn B. Structural and functional studies of Hemoglobin Barcelona (α2β2 94 Asp (FG1)His). J. Mol. Biol 1982; 156: 185
   PubMed Web of Science ®Google Scholar
• Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., Chevrier M., Bordahandy C., Rosa J. Hemoglobin Saint Mande (β102 (G4) AsnTyr: A new low oxygen affinity variant. FEBS Lett 1981; 126: 114
   PubMed Web of Science ®Google Scholar
• Gibb E. A. Increased subunit association of a new superstable variant Hemoglobin Motown. Clin. Res 1981; 29: 795A
   Google Scholar
• Ohta Y., Saito S., Fujita S., Wilson J. B., Lam H., Huisman T. H. J. HbF‐Meinohama or α2γ2(5 GluGly; 75 Ile 136Gly). Hemoglobin 1981; 5: 565
   PubMed Web of Science ®Google Scholar
• Yoshinaka H., Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K. A new y chain variant, Hb F Kotobuki or AγI 6 (A3) GluGly. Hemoglobin 1982; 6: 37
   PubMed Web of Science ®Google Scholar
• Johnson C. S., Schroeder W. A., Shelton J. B., Shelton J. R. The first example of a deletion in the human a chain: Hemoglobin Boyle Heights or α 6(A4) Asp0 β2. Hemoglobin 1983; 7: 125
   PubMed Web of Science ®Google Scholar
• Sugihara J., Imamura T., Yamada H., Imoto T., Matsuo T., Sumida I., Yanase T. A new electrophoretic variant of hemoglobin (Ogi) in which a leucine residue is replaced by an arginine residue at position 34 of the α‐chain. Biochim. Biophys. Acta 1982; 701: 45
   PubMed Web of Science ®Google Scholar
• Ricco G., Mazza U., Turi R. M., Pich P. G., Camaschella C., Saglio G., Bernini L. F. Significance of a new type of human fetal hemoglobin carrying a replacement isoleucinethreonine at position 75 (E19) of the γ chain. Hum. Genet 1976; 32: 305
   PubMed Web of Science ®Google Scholar
• Webber B. B., Lam H., Wilson J. B., Huisman T. H. J. Hb Albany‐GA or α2 11 (A9) LysAsn β2. Hemoglobin 1983; 7: 257
   PubMed Web of Science ®Google Scholar
• Honig G. R., Shamsuddin M., Vida L. N., Mompoint M., Bowie L., Jones E., Well S. Hb Evanston (αl4 TrpArg): A new variant with thalassemia‐like hematologic expression. Blood 1982; 60(Suppl. 1)53a
   Google Scholar
• Liang C. ‐C., Chen S., Yang K., Jia P., Ma Y., Li T., Ni X., Wang X., Deng Q., Yao S. Hemoglobin Beijing ‘α16 (A14) LysAsn’: A new fast‐moving hemoglobin variant. Hemoglobin 1982; 6: 629
   PubMed Web of Science ®Google Scholar
• Sellaye M., Blouquit Y., Galacteros F., Arous N., Monplaisir N., Rhoda M. D., Braconnier F., Rosa J. A new silent hemoglobin variant in a Black family from French West Indies. Hemoglobin Le Lamentin α20 HisGln. FEBS Lett 1983; 145: 128
   Web of Science ®Google Scholar
• Zeng Y. ‐T., Huang S. ‐Z., Zhou X. ‐D., Qui X. ‐K., Dong Q. ‐Y., Li M. ‐Y., Bai J. ‐H. Hb Shenyang ‘α26 (B7) AlaGlu’: A new unstable variant found in China. Hemoglobin 1982; 6: 625
   PubMed Web of Science ®Google Scholar
• Dysert P. A., II, Head C. G., Shih T. B., Jones R. T., Schneider R. G. Hb Dallas α2 97 (G4) AsnLys β2: A new abnormal hemoglobin with high oxygen affinity. Blood 1982; 60(Suppl. 1)53a
   Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hemoglobin Tokoname ‘α139 (HC1) LysThr’: A new hemoglobin variant with a slightly increased oxygen affinity. Hemoglobin 1983; 7: 85
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Imai K., Seki M. Hemoglobin Machida ‘β6 (A31 GluGln’, a new abnormal hemoglobin discovered in a Japanese family: structure, function and biosynthesis. Hemoglobin 1982; 6: 531
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Johnson M. H., McGuffey J. E., Jue D. L., Therrell B. L., Jr. Hemoglobin Rio Grande ‘β8 (A5) LysThr’, a new variant found in a Mexican‐American family. Hemoglobin 1983; 7: 91
   PubMed Web of Science ®Google Scholar
• Elion J., Wajcman H., Belkhodja‐Dunda O., Lapoumeroulie C., Labie D., Messerschmitt J., Staal A. M., Desableno B. Hemoglobin J Amiens, Beta 17 (A14) Lys replaced by Asn. Coincidence of a functionally silent new abnormal hemoglobin and a polycythemia vera. Nouv. Rev. Fr. d'Hematol 1979; 21: 347
   PubMedGoogle Scholar
• Brennan S. O., Williamson D., Whisson M. E., Carrell R. W. Hemoglobin Palmerston North β23 (B5) ValPhe a new variant identified in a patient with polycythemia. Hemoglobin 1982; 6: 569
   PubMed Web of Science ®Google Scholar
• Arous N., Galacteros F., Fessas Ph., Loukopoulos D., Blouquit Y., Komis G., Sellaye M., Boussiou M., Rosa J. Structural study of Hemoglobin Knossos, β27 (B9) AlaSer. A new abnormal hemoglobin present as a silent β‐thalassemia. FEBS Lett 1982; 147: 247
   PubMed Web of Science ®Google Scholar
• Boissel J. P., Wajcman H., Labie D., Fabritius H., Cabannes R. Hb J Daloa ‘β57 (E1) AsnAsp’: A new variant found in Ivory Coast. Hemoglobin 1982; 6: 433
   PubMed Web of Science ®Google Scholar
• Como P. F., Kennett D., Wilkinson T., Kronenberg H. A new hemoglobin with high oxygen affinity Hemoglobin Bunbury: α2β2 ‘94 (FG1) AspAsn’. Hemoglobin 1983; 7: 413
   PubMed Web of Science ®Google Scholar
• Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., Miyaji T. Hemoglobin Saitama or β117 (G19) HisPro, a new variant causing hemolytic dis‐ease. Hemoglobin 1983; 7: 47
   PubMed Web of Science ®Google Scholar
• Lu Y. ‐Q., Fan J. ‐L., Liu J. ‐F., Hu H. ‐L., Peng X. ‐H., Huang P. ‐Y., Chen S. ‐S., Jia P. ‐C., Yang K. ‐G., Liang C. ‐C., Ren X. ‐D., Zuo C. ‐R. Hemoglobin Jianghua ‘β120 (GH3) LysIle’: A new fast‐moving variant found in China. Hemoglobin 1983; 7: 321
   PubMed Web of Science ®Google Scholar
• Kamel K., El‐Najjar A., Webber B. B., Chen S. S., Wilson J. B., Kutlar A., Huisman T. H. J. Hb Doha or α2β2 ‘X‐N‐Met‐1(NA1) ValGlu’; a new β chain abnormal hemoglobin observed in a Qatari female. Biochim. Biophys. Acta 1985; 831: 257
   PubMed Web of Science ®Google Scholar
• Salkie M. L., Gordon P. A., Rigal W. M., Lam H., Wilson J. B., Head‐lee M. E., Huisman T. H. J. Hb A2‐Canada or αδ99 (G1) AspAsn, a newly discovered delta chain variant with increased oxygen affinity occurring in cis to β‐thalassemia. Hemoglobin 1982; 6: 223
   PubMed Web of Science ®Google Scholar
• Juricic D., Crepinko I., Efremov G. D., Lam H., Webber B. B., Headlee M. G., Huisman T. H. J. Hb A2 Zagreb or α2δ2 125 (H3) GlnGlu in association with δβ‐thalassemia in a Yugoslavian female. Hemoglobin 1983; 7: 443
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Webber B., Lam H., Wilson J. B., Huisman T. H. J., Sciarratta G. V., Sansone G., Molaro G. L. A new y chain variant: Hb F‐Pordenone ‘γ6 (A3) GIuGln: 75 He: 136 Ala’. Hemoglobin 1982; 6: 397
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Headlee M., Lam H., Wilson J. B., Huisman T. H. J. Hb F‐Bonaire‐Ga or α2Aβ2 39 (C5) GlnArg, characterized by high pressure liquid chromatographic and microsequencing procedures. Hemoglobin 1982; 6: 599
   PubMed Web of Science ®Google Scholar
• Honig G. R., Koshy M., Schroeder W. A., Shelton J. B., Shelton J. R. Hemoglobin F Lodz (GγI 44 SerArg) a newly identified variant from an American infant of Polish descent. Biochim. Biophys. Acta 1982; 707: 213
   PubMed Web of Science ®Google Scholar
• Serjeant G. R., Serjeant B. E., Lehmann H., Dukes M., Robb L. Hb F Kingston ‘Gγ 55 (D6) MetArg’. FEBS Lett 1982; 150: 77
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Lam H., Huisman T. H. J. Hb F‐Kennestone or α2Gγ2 (EF1) 77 HisArg observed in a Caucasian baby. Hemoglobin 1983; 7: 267
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Lam H., Carver J., Huisman T. H. J. Hb F‐Marietta or GγI 80 ‘EF4’ AspAsn, observed in a Caucasian baby. Hemoglobin 1982; 6: 407
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Lam H., Wilson J. B., Webber B. B., Huisman T. H. J. Hb F‐Columbus‐Ga or α2Gγ2 94 (FG1) AspAsn. Hemoglobin 1982; 6: 593
   PubMed Web of Science ®Google Scholar
• Shelton J. B., Shelton J. R., Espinueva Z., Huynh V., Schroeder W. A., Powars D. Hemoglobin F‐Caltech: α2Gγ2 120 LysGln. Hemoglobin 1982; 6: 577
   PubMed Web of Science ®Google Scholar
• Care A., Marinucci M., Massa A., Maffi D., Sposi N. M., Improta T., Tentori L. Hb F‐Siena ‘α2AγT2 121 (GH4) GlyLys’. A new fetal hemoglobin variant. Hemoglobin 1983; 7: 79
   PubMed Web of Science ®Google Scholar
• Honig G. R. 1982, Personal Communication
   Google Scholar
• Bradley T. B. 1982, Personal Communication
   Google Scholar
• McDonald M. J., Noble R. W., Sharma V. S., Ranney H. M., Crookston J. H., Schwartz J. M. A comparison of the functional properties of two Lepore hemoglobins with those of Hemoglobin A1. J. Mol. Biol 1975; 94: 305
   PubMed Web of Science ®Google Scholar
• Sugihara J., Imamura T., Kagimoto M., Matsuo T., Yamada H., Imoto T., Yanase T. A new electrophoretic variant of hemoglobin (Munakata) in which a lysine residue is replaced by a methionine residue at position 90 of the α chain. Biochim. Biophys. Acta 1983; 744: 119
   PubMed Web of Science ®Google Scholar
• Ohya Y. Abnormal hemoglobins in North‐Kyushu Japan, with special reference to Hb‐Kukura and Hb‐Fukuoka. Jap. J. Hum. Genet 1963; 8: 23
   Google Scholar
• Moo‐Penn W. F., Bechtel K. C., Therrell B. L. Hemoglobin β Nilotic in a Mexican‐American family. Hemoglobin 1978; 2: 65
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Milner P. F. Haemoglobin Constant Spring ‐ a chain termination mutant?. Nature 1971; 234: 337
   PubMed Web of Science ®Google Scholar
• Strahler J. R., Rosenbloom B. B., Hanash S. M. A silent, neutral substitution detected by reverse‐phase high‐performance liquid chromatography: Hemoglobin Beirut. Science 1983; 221: 860
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Mori H., Arimasa N. Hemoglobin Okayama ‘β2 (NA2) HisKiln’: a new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3 diphosphoglycerate binding site. FEBS Lett 1983; 156: 20
   PubMed Web of Science ®Google Scholar
• Wilkinson T., Gough P., Owen M. C., Carrell R. W., Kronenberg H. Detection of variants of haemoglobin D in Australia: Haemoglobin D Camperdown α2β2 121 GluVal and Haemoglobin D Punjab α2β2 121 GluGln. Med. J. Aust 1974; 2: 636
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Wang C. ‐L. Hemoglobin New York in Chinese subjects in Taiwan. Am. J. Phys. Anthropol 1971; 34: 329
   PubMed Web of Science ®Google Scholar
• Wajcman H., Jones R. T. Proprietes fonctionelles des hemoglobins humaines mutees en position β73. INSERM 1977; 70: 269
   Google Scholar
• Shimasaki S., Iuchi I., Hidaka K., Mizuta W. The survey of abnormal hemoglobin in Kobe district. Jap. J. Hum. Genet 1983; 28: 127
   Google Scholar
• Marinucci M., Boissel J. P., Massa A., Wajcman H., Tentori L., Labie D. Hemoglobin Maputo: a new β‐chain variant (α2β2 47 (CD6) AspTyr) in combination with Hb S, identified by high performance liquid chromatography (HPLC). Hemoglobin 1983; 7: 423
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Imai K., Tsuneshige A., Yamada H., Seki M., Fukui H. Hemoglobin Kariya ‘α40 (C5) LysGlu’ a new hemoglobin variant with an increased oxygen affinity. FEBS Lett 1983; 153: 332
   PubMed Web of Science ®Google Scholar
• Kohne E., Behnken L. J., Leupold D., Rogge H., Martin H., Kleihauer E. Hemoglobin Presbyterian ‘β108 (G10) AsnLys’ in a German family. Hemoglobin 1979; 3: 365
   PubMed Web of Science ®Google Scholar
• Como P. F., Barber S., Sage R. E., Trent R. J., Kronenberg H. Hemoglobin Woodville: α6 (A4) Aspartic AcidTyrosine. Hemoglobin 1986; 10: 135
   PubMed Web of Science ®Google Scholar
• Sugihara J., Imamura T., Yamada H., Imoto T., Matsuo T., Sumida I., Yanase T. A new electrophoretic variant of hemoglobin (Ogi) in which a leucine residue is replaced by an arginine residue at position 34 of the α‐chain. Biochim. Biophys. Acta 1982; 701: 45
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Wilson J. B., Huisman T. H. J. Hb Cordele α2 47 (CE5) AspAla β2 a mildly unstable variant observed in Black twins. Hemoglobin 1984; 8: 37
   PubMed Web of Science ®Google Scholar
• Wong S. C., Ali M. A. M., Pond J. R., Rubin S. M., Johnson S. E. N., Wilson J. B., Huisman T. H. J. Hb J‐Singa (α‐78 AsnAsp), a newly discovered hemoglobin variant with the same amino acid substitution as one of the two present in Hb J‐Singapore (α‐78 AsnAsp, α‐79 AlaGly). Biochim. Biophys. Acta 1984; 784: 187
   PubMed Web of Science ®Google Scholar
• Sciarratta G. V., Ivaldi G., Parodi M. I., Sansone G., Molaro G. L., Salkie M. L., Wilson J. B., Reese A. L., Huisman T. H. J. The characterization of Hemoglobin Manitoba or α2 102 (G9) SerArg β2 and Hemoglobin Contaldo or α2 103 (G10) HisArg β2 by high performance liquid chromatography. Hemoglobin 1984; 8: 169
   PubMed Web of Science ®Google Scholar
• Cai Y. ‐L., Wang H. ‐B., Yang X. ‐Y., Liu Z. ‐H., Ao Z. ‐F., Gong D. ‐H., Ma J. ‐P., Wang M. ‐L., Ma D. ‐R., Xu Y. ‐Q., Chen E. ‐H. A new fast‐moving hemoglobin variant, Hb J Luhe β8 (A5) LysGln. Chinese Hematol. J 1982; 3: 263
   Google Scholar
• Wong S. C., Ali M. A. M., Lam H., Webber B. B., Wilson J. B., Huisman T. H. J. Hemoglobin Hamilton or α2β2 11 (A8) ValIle, a silent β‐chain variant detected by Triton X‐100 acid‐urea polyacrylamide gel electrophoresis. Am. J. Hematol 1984; 16: 47
   PubMed Web of Science ®Google Scholar
• Williamson D., Brennan S. O., Muir H., Carrell R. W. Hemoglobin Collingwood β60 (E4) ValAla ‐ a new unstable hemoglobin. Hemoglobin 1983; 7: 511
   PubMed Web of Science ®Google Scholar
• Jen P. C., Chen L. C., Chen P. F., Wong Y., Chen L. F., Guo Y. Y., Chang F. Q., Chow Y. C., Chiu Y. Hemoglobin Quin‐Hai, β78 (EF2) LeuArg, a new abnor‐mal hemoglobin found in Guangdong, China. Hemoglobin 1983; 7: 407
   PubMed Web of Science ®Google Scholar
• Hedlund B., Paine S., Smith C. M., II, Raines J., Morrison W. T., Adams J., III. Hemoglobin Minneapolis‐Laos ‘β‐118 (GH1) PheTyr’ a new hemoglobin variant with normal functional properties. Hemoglobin 1984; 8: 75
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Williamson D., Smith M. B., Cauchi M. N., Macphee A., Carrell R. W. Hb A2 Victoria δ24 (B6) GlyAsp, a new δ chain variant occurring with δ‐thal‐assemia. Hemoglobin 1984; 8: 163
   PubMed Web of Science ®Google Scholar
• Garcia C. R., Navarro J. L., Lam H., Webber B. B., Headlee M. G., Wilson J. B., Huisman T. H. J. Hb A2‐Manzanares or α2δ2 121 (GH4) GluVal, an unstable δ chain variant observed in a Spanish family. Hemoglobin 1983; 7: 435
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Lam H., Huisman T. H. J. Hb F‐Calluna or α2γ2 (12 ThrArg; 75 Ile; 136 Ala) in a Caucasian baby. Hemoglobin 1983; 7: 563
   PubMed Web of Science ®Google Scholar
• Zeng Y. T., Huang S. Z., Nakatsuji T., Huisman T. H. J. ‐gγAγ‐Thalassemia and γ‐chain variants in Chinese newborn babies. Am. J. Hematol 1985; 18: 235
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Shimizu K., Huisman T. H. J. Hb F‐La Grange or α2γ2 101 (G3) GluLys; 75 Ile; 136 Gly; a high oxygen affinity fetal hemoglobin variant observed in a Caucasian newborn. Biochim. Biophys. Acta 1984; 789: 224
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Thillet J., Beuzard Y., Vernant J. P., Dreyfus B. Structural and functional studies of Hemoglobin J Calabria: P64 (E8) GlyAsp. Biochim. Biophys. Acta 1977; 492: 426
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Baine R. M., Jue D. L., Johnson M. H., McGuffey J. E., Benson J. M. Hemoglobin Evanston: α14 (A12) TrpArg, a variant hemoglobin associated with α‐thalassemia‐2. Biochim. Biophys. Acta 1983; 747: 65
   PubMed Web of Science ®Google Scholar
• Wada Y., Hayashi A., Masanori I., Katakuse T., Ichihara H., Nakabushi T., Matsuo T., Sakurai T., Matsuda H. Characterization of a new fetal hemoglobin variant, Hb F‐Izumi Aγ6 GluGly, by molecular secondary ion mass spectrometry. Biochim. Biophys. Acta 1983; 749: 244
   PubMed Web of Science ®Google Scholar
• Rochette J., Poyart C., Varet B., Wajcman H. A new hemoglobin variant altering the α1β2 contact: Hb Chemilly (X2P2 99 (G1) AspVal. FEBS Lett 1984; 166: 8
   PubMed Web of Science ®Google Scholar
• Rochette J., Varet B., Boissel J. P., Clough K., Labie D., Wajcman H., Bohn B., Magne P., Poyart C. Structure and function of Hb Saint‐Jacques ((α2β2 140 (H18) AlaThr): A new high oxygen‐affinity variant with altered bisphosphoglycerate binding. Biochim. Biophys. Acta 1984; 785: 14
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Mori H., Seki M. Hemoglobin Aichi ‘α50 (CE8) HisArg’: A new slightly unstable hemoglobin variant discovered in Japan. FEBS Lett 1984; 169: 297
   PubMed Web of Science ®Google Scholar
• Chih‐chuan L., Fei X., Kegong Y., Song‐sen C., Peichen J., Maoqi Z., Zhiheng Z. Hemoglobin GuiZhou or α2 77 (EF6) ProArg β2, a new slow‐moving hemoglobin variant observed in China. Hemoglobin 1984; 2: 387
   Google Scholar
• Zeng Y. ‐T., Huang S. ‐Z., Qiu X. ‐K., Cheng G. ‐C., Ren Z. ‐R., Jin Q. ‐C., Chen C. ‐Y., Jiao C. ‐T., Tang Z. ‐G., Liu R. ‐H., Bao X. ‐H., Zeng L. ‐Z., Duan Y. ‐Q., Zhang G. ‐Y. Hemoglobin Chongqing (α2 (NA2) LeuArg) and Hemoglobin Harbin (α 16 (A 14) LysMet) found in China. Hemoglobin 1984; 8: 569
   PubMed Web of Science ®Google Scholar
• Houjun L., Dexiang L., Zhiguo L., Ping L., Ly L., Ji C., Shaozhi H. A new fast‐moving hemoglobin variant, Hb J‐Tashikuergan α19 (AB1) AlaGlu. Hemoglobin 1984; 8: 391
   PubMed Web of Science ®Google Scholar
• Jeppsson J. O., Kallman L., Lindgren G., Fagerstam L. G. Hb Linkoping (β36 ProThr): a new hemoglobin mutant characterized by reversed‐phase high performance liquid chromatography. J. Chromatogr 1984; 297: 31
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Delanoe‐Garin J., Lacombe C., Arous N., Cayre Y., Peduzzi J., Braconnier F., Galacteros F. Structural study of hemoglobin Hazebrouck, β38 (C4) ThrPro: A new abnormal hemoglobin with instability and low oxygen affinity. FEBS Lett 1984; 172: 155
   PubMed Web of Science ®Google Scholar
• Rahbar S., Asmerom Y., Blume K. G. A silent hemoglobin variant detected by HPLC: Hemoglobin City of Hope β69 (E13) GlySer. Hemoglobin 1984; 8: 333
   PubMed Web of Science ®Google Scholar
• Williamson D., Brennan S. O., Strosberg H., Whitty J., Carell R. W. Hemoglobin α2 Fitzroy δ142 AlaAsp: A new delta‐chain variant. Hemoglobin 1984; 8: 325
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Johnson M. H., McGuffey J. E., Jue D. L. Hemoglobin Shelby ‘β131 (H9) GlnLys’: A correction to the structure of Hemoglobin Deaconess and Hemoglobin Leslie. Hemoglobin 1984; 8: 583
   PubMed Web of Science ®Google Scholar
• Harano K., Harano T., Shibata S., Ueda S., Mori H., Seki M. Hb Okazaki β93 (F8) CysArg’, a new hemoglobin variant with increased oxygen affinity and instability. FEBS Lett 1984; 173: 45
   PubMed Web of Science ®Google Scholar
• Jones R. T., Head C., Shih M. F.‐C., Shih D. T. ‐B., Dana B., Jones M. B., Koler R. D. Hemoglobin Linkoping ‘β36 (C2) ProThr’ in a large Finnish family from Astoria, Oregon, USA. Hemoglobin 1986; 10: 455
   PubMed Web of Science ®Google Scholar
• Jones R. T., Barwick R. C., Head C. G., Shih F. C., Shih T. B. Hemoglobin Long Island. Abstract #151. 20th Congress of International Society of Haematology. Buenos AiresArgentina 1984
   Google Scholar
• Delanoe‐Garin J., Blouquit Y., Arous N., Kister J., Poyart C., North M. L., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Saverne: a new variant with elongated β chains: structural and functional properties. Hemoglobin 1988; 12: 337
   PubMed Web of Science ®Google Scholar
• Wilson C. I. D., Cave R. J., Lehmann H., Close M., Imai K. Haemoglobin Warwickshire (β5 ‘A2’ ProArg): A possible ‘fine tuning’ of 2,3‐DPG affinity by β5 Pro. FEBS Lett 1984; 176: 331
   PubMed Web of Science ®Google Scholar
• Guis M., Mentzer W. C., Jue D. L., Johnson M. H., McGuffey J. E., Moo‐Penn W. F. Hemoglobin Twin Peaks α113 (GH1) LeuHis. Hemoglobin 1985; 9: 175
   PubMed Web of Science ®Google Scholar
• Chen S. S., Webber B. B., Wilson J. B., Huisman T. H. J. Hb Gainesville‐GA or α2β2 46 (CD5) GlyArg. Hemoglobin 1985; 9: 179
   PubMed Web of Science ®Google Scholar
• Delanoe‐Garin J., Arous N., Blouquit Y., Hafsia R., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Kenitra
   Google Scholar
• Devaraj R., Wilson J. B., Huisman T. H. J. Hb Regina or α2β2 96 (FG3) LeuVal, a high oxygen affinity variant discovered by cation‐exchange HPLC. Am. J. Hematol 1985; 19: 195
   PubMed Web of Science ®Google Scholar
• Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., Shibata K., Shimokata H., Kuzuya F., Miwa S. A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or β97 (FG4) HisPro. Hemoglobin 1985; 9: 11
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Webber B. B., Huisman T. H. J. Hb Leslie is the same as Hb Shelby or α2β2 131 (H9) GlnLys. Hemoglobin 1984; 8: 595
   PubMed Web of Science ®Google Scholar
• Chen S. S., Wilson J. B., Webber B. B., Huisman T. H. J., Miwa S., Amenomori Y. Hb F‐Tokyo or α2Gγ234 (B16) ValIle, a silent y chain variant detected by reverse phase high performance liquid chromatography. Hemoglobin 1985; 9: 25
   PubMed Web of Science ®Google Scholar
• Chen S. S., Wilson J. B., Huisman T. H. J. Hb F‐Pendergrass, an Aγ1 variant with a ProArg substitution at position γ36 (C2). Hemoglobin 1985; 9: 73
   PubMed Web of Science ®Google Scholar
• Al‐Awamy B. H., Niazi G. A., Al‐Mouzan M. I., Chen S. S., Wilson J. B., Webber B. B., Huisman T. H. J. Hb F‐Damman or α2Aγ2 79 (EF3) AspAsn. Hemoglobin 1985; 9: 171
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Lena‐Russo D., Delanoe J., Arous N., Bardakdjian J., Lacombe C., Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille α2β2 1 (A1) NH2‐Met, 2 (A2) His3 (A3) Pro: First variant having a N‐terminal elongated β chain. Blood 1984; 64(Suppl. 1)55a
   Google Scholar
• Shimasaki S. A new hemoglobin variant, Hemoglobin Nunobiki ‘α141 (HC3) ArgCys’. Notable influence of the carboxy‐terminal cysteine upon various physico‐chemical characteristics of hemoglobin. J. Clin. Invest 1985; 75: 695
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Morrison W. T., Pullen D. J., Abney R. L., III, Steinberg M. H. Hemoglobin Mississippi (MS): a new hemoglobin variant with three distinct electrophoretic mobilities. Clin. Res 1985; 33: 603A
   Google Scholar
• Merault G., Keclard L., Saint‐Martin C., Jasmin K., Campier A., Delanoe‐Garin J., Arous N., Fortune R., Theodore M., Seytor S., Rosa J., Blouquit Y., Galacteros F. Hemoglobin Roseau‐Pointe a Pitre α2β2 90 (F6) GluGly: a new hemoglobin variant with slight instability and low oxygen affinity. FEBS Lett 1985; 184: 10
   PubMed Web of Science ®Google Scholar
• Como P. F., Hocking D., Trent R. J., Kronenberg H. Hb Geelong: β2139 (H17) AsnAsp. A new hemoglobin with thalassemia‐like characteristics. Presented as abstract at February meeting of N. S. W. Thalassemia Society. 1985
   Google Scholar
• Barwick R. C., Jones R. T., Head C. G., Shih M. F.‐C., Prchal J. T., Shih D. T.‐B. Hb Long Island: A hemoglobin variant with a methionyl extension at the NH2 terminus and a prolyl substitution for the normal histidyl residue 2 of the β chain. Proc. Natl. Acad. Sci. USA 1985; 82: 4602
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Arous N., Lena D., Delanoe‐Garin J., Lacombe C., Bardakdjian J., Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille ‘α2β2 N methionyl‐2 (NA2) HisProj: a new β chain variant having an extended N‐terminus. FEBS Lett 1984; 178: 315
   PubMed Web of Science ®Google Scholar
• Shelton J. B., Shelton J. R., Schroeder W. A., Powars D. R. Hb Aztec or α276 (EF5) MetThrβ2 detection of a silent mutant by high performance liquid chromatography. Hemoglobin 1985; 9: 325
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S. Hb Owari ‘α121 (H4) ValMet’: a new hemoglobin variant with a neutral‐to‐neutral amino acid substitution detected by isoelectric focusing. Hemoglobin 1986; 10: 127
   PubMed Web of Science ®Google Scholar
• Bowman J. E., Bloom R., Chen S. ‐S., Webber B. B., Wilson J. B., Kutlar F., Kutlar A., Huisman T. H. J. Hb Chicago or α2 136 (H19) LeuMet β2. Hemoglobin 1986; 10: 495
   PubMed Web of Science ®Google Scholar
• Rahbar S., Louis J., Lee T., Asmerom Y. Hemoglobin North Chicago (β36 ‘C2’ ProlineSerine): A new high affinity hemoglobin. Hemoglobin 1985; 9: 559
   PubMed Web of Science ®Google Scholar
• Huisman T. H. J., Wilson J. B., Kutlar A., Yang K. ‐G., Chen S. ‐S., Webber B. B., Altay C., Martinez Villegas A. Hb J‐Antakya or α2β2 65 (E9) LysMet in a Turkish family and Hb Complutense or α2β2 127 (H5) GinGlu in a Spanish family; correction of a previously published identification. Biochim. Biophys. Acta 1986; 871: 229
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Imai N., Kitazumi T. A new electrophoretically‐silent hemoglobin variant: Hemoglobin Kofu or α2β2 84 (EF8) ThrIle. Hemoglobin 1986; 10: 417
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K. Hb Himeji or β140 (H18) AlaAsp, a slightly unstable hemoglobin with increased N‐terminal glycation. Hemoglobin 1986; 10: 109
   PubMed Web of Science ®Google Scholar
• Harano K., Harano T., Ueda S., Ohkushi T., Imai K. A new hemoglobin variant, Hb Mito ‘β144 (HC1) LysGlu’, with increased oxygen affinity. FEBS Lett 1985; 192: 75
   PubMed Web of Science ®Google Scholar
• Ohba Y., Igarashi M., Tsukahara M., Nakashima M., Sanada C., Ami M., Arai Y., Miyaji T. Hb A Yokoshima, α2β225 (B7) GlyAsp, a new δ chain variant found in a Japanese Family. Hemoglobin 1985; 9: 613
   PubMed Web of Science ®Google Scholar
• Fujita S., Ohta Y., Saito S., Kobayashi Y., Naritomi Y., Kawaguchi T., Imamura T., Wada Y., Hayashi A. Hemoglobin A2 Honai (α2β290 (F6) GluVal): A new delta chain variant. Hemoglobin 1985; 9: 597
   PubMed Web of Science ®Google Scholar
• Hu H., Ma M. Hb F‐Urumqi GγI 22 (B4) AspGly: a new fetal hemoglobin variant found in a Uygur baby. Hemoglobin 1986; 10: 15
   PubMed Web of Science ®Google Scholar
• Chen S. ‐S., Webber B. B., Kutlar A., Wilson J. B., Huisman T. H. J. Hb F‐Cobb or α2Aγ237 (C3) TrpGly. Hemoglobin 1985; 9: 617
   PubMed Web of Science ®Google Scholar
• Chen S. ‐S., Wilson J. B., Webber B. B., Huisman T. H. J. Hb F‐Beech Island or α2β253 (D4) AlaAsp. Hemoglobin 1985; 9: 525
   PubMed Web of Science ®Google Scholar
• Boissel J. ‐P., Kasper T. J., Shah S. C., Malone J. I., Bunn H. F. Amino‐terminal processing of proteins: Hemoglobin South Florida, a variant with retention of initiator methionine and Nα‐acetylation. Proc. Natl. Acad. Sci. USA 1985; 82: 8448
   PubMed Web of Science ®Google Scholar
• Barwick R. C., Head C. G., Shih M. F.‐C., Block S. H., Jones R. T. Hb T‐Cambodia ‘beta 26 (B8) GluLys, beta 121 (GH4) Glu Gin’: a new doubly substituted beta globin variant found in a Cambodian family. Blood 1985; 66(Suppl. 1)68a
   Google Scholar
• Moo‐Penn W. F., McGuffey J. E., Jue D. L., Johnson M. H., Schum T. Hemoglobin New Mexico: β100(G2)ProArg. A variant hemoglobin associated with erythrocytosis (BBA 32356). Biochim. Biophys. Acta 1985; 832: 192
   PubMed Web of Science ®Google Scholar
• Lacombe C., Craescu C. T., Blouquit Y., Kister J., Poyart C., Delanoe‐Garin J., Arous N., Bardakdjian J., Riou J., Rosa J., Schaeffer C., Galacteros F. Structural and functional studies of hemoglobin Poissy α2β2 56 (D7) GlyArg and 86 (F2) AlaPro. Eur. J. Biochem 1985; 153: 655
   PubMedGoogle Scholar
• Como P. F., Raven J. L., Wilkinson T., Kronenberg H. Comparison of the six hemoglobin variants occurring at the α6 (A4) position with particular reference to the α6 AspGly substitution found in Perth. Haematology Society of Australia, Western Australia October, 1984, Perth, Western Australia
   Google Scholar
• Chen S. S., Webber B. B., Wilson J. B., Huisman T. H. J. Hb F‐Forest Park, a new Aγ variant with two amino acid substitutions, 75(E19)IleThr and 73(E17)AspAsn, which can be identified in adults by gene‐mapping analysis. Biochim. Biophys. Acta 1985; 832: 242
   PubMed Web of Science ®Google Scholar
• Wada Y., Fujita T., Kidoguchi K., Hayashi A. Fetal hemoglobin variants in 80,000 Japanese neonates: High prevalence of Hb F Yamaguchi (AγT80AspAsn). Hum. Genet 1986; 72: 196
   PubMed Web of Science ®Google Scholar
• Monplaisir N., Merault G., Poyart C., Rhoda M. D., Craescu C. T., Vidaud M., Galacteros F., Blouquit Y., Rosa J. Hb S Antilles (α2β2 6 GluVal, 23 ValIleu): A new variant with lower solubility than Hb S and producing sickle cell disease in heterozygotes. Proc. Natl. Acad. Sci. USA 1986; 83: 9363
   PubMed Web of Science ®Google Scholar
• Ogata K., Ito T., Okazaki T., Dan K., Nomura T., Nozawa Y., Kajita A. Hemoglobin Sendagi (β42 PheVal): a new unstable hemoglobin variant having an amino acid substitution at CD1 of the β‐chain. Hemoglobin 1986; 10: 469
   PubMed Web of Science ®Google Scholar
• Baiget M., Gomez Pereira C., Jue D. L., Johnson M. H., McGuffey J. E., Moo‐Penn W. F. A case of Hemoglobin Indianapolis ‘(β112 (G14) CysArg’ in an individual from Cordoba, Spain. Hemoglobin 1986; 10: 483
   PubMed Web of Science ®Google Scholar
• De Pablos J. Ma., Wilson J. B., Kutlar A., Chen S. S., Huisman T. H. J. HbF‐Albaicin or Gγ8(AS)LysGlu or Gln. Hemoglobin 1986; 10: 655
   PubMed Web of Science ®Google Scholar
• Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Gonzalez Redondo J. M., Huisman T. H. J. Hb F‐Clarke or α2Gγ265(E9)LysAsn. Hemoglobin 1987; 11: 185
   PubMed Web of Science ®Google Scholar
• Kleman K., Lubin B., Wilson J. B., Kutlar A., Webber B. B., Huisman T. H. J. Hb F‐Oakland or α2Gγ1226)B8)GluLys. Hemoglobin 1987; 11: 181
   PubMed Web of Science ®Google Scholar
• Indrak K., Wiedemann B. F., Batek F., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H. J. Hb Olomouc or α2β286(F2)AlaAsp, a new high oxygen affinity variant. Hemoglobin 1987; 11: 151
   PubMed Web of Science ®Google Scholar
• Jen P. C., Liu Y. Hemoglobin Guangzhou, α64(E13)AspGly, a new abnormal hemoglobin found in Guangzhou, China. Hemoglobin 1987; 11: 23
   Web of Science ®Google Scholar
• Zhou Z. ‐Q., Chen L. ‐C., Chen P. ‐F., Zhang K. ‐Q., Wang Y. ‐H. Hemoglobin Hangzhou, α64(E13)AspGly, anew variant found in China. Hemoglobin 1987; 11: 31
   PubMed Web of Science ®Google Scholar
• Ohba Y., Yamamoto K., Kawata R., Miyaji T. Hyperunstable Hemoglobin Toyama α2136 (H19) LeuArg β2 detection and identification by in vitro biosynthesis with radioactive amino acids. Hemoglobin 1987; 11: 539
   PubMed Web of Science ®Google Scholar
• Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., Galacteros F., Feingold J., Rosa J. Hemoglobin La Desirade αA2β2 129 (H7) AlaVal: A new unstable hemoglobin. Hemoglobin 1986; 10: 593
   PubMed Web of Science ®Google Scholar
• Fleming P. J., Sumner D. R., Wyatt K., Hughes W. G., Melrose W. D., Jupe D. M. D., Baikie M. J. Hemoglobin Hobart or α20(B1)HisArg: A new α chain hemoglobin variant. Hemoglobin 1987; 11: 211
   PubMed Web of Science ®Google Scholar
• Williamson D., Wells R. M. G., Anderson R., Matthews J. Anew unstable and low oxygen affinity hemoglobin variant: Hb J‐Auckland ‘β25(B7)GlyAsp’. Hemoglobin 1987; 11: 221
   PubMed Web of Science ®Google Scholar
• Masala B., Manca L., Stangoni A., Cuccuru G. B., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H. J. Hb Sassari or α2126 (H9) AspHisβα observed in a family from Northern Sardinia. Hemoglobin 1987; 11: 373
   PubMed Web of Science ®Google Scholar
• Shih D. T.‐B., Jones R. T., Shih M. F.‐C., Jones M. B., Koler R. D., Howard J. Hemoglobin Chico ‘β66(E10)LysThr’: a new variant with decreased oxygen affinity. Hemoglobin 1987; 11: 453
   PubMed Web of Science ®Google Scholar
• Hu H., Ma M. Hb F‐Xinjiang or Aγ225(B7)GlyArg: a new slow‐moving unstable fetal hemoglobin variant. Hemoglobin 1987; 11: 465
   PubMed Web of Science ®Google Scholar
• Ma M., Hu H., Kutlar F., Wilson J. B., Huisman T. H. J. Hb F‐Xin‐Su or AγT73(E17)AspHis: a new slow‐moving fetal hemoglobin variant. Hemoglobin 1987; 11: 473
   PubMed Web of Science ®Google Scholar
• Como P. F., Hocking D., Trent R. A., Wilkinson T., Wylie B. R., Bruce D., Kronenberg H. Hb Geelong ((β139 AsnAsp) and Hb Stanmore (β111 ValAIa). Two new unstable haemoglobins which illustrate the problem of distinguishing a haemoglobin with a thalassaemic phenotype from one inherited along with beta‐thalassemia in either cis or trans. Book of Abstracts XXI Congr. Internatl. Soc. Haematol, and XIX Congr. Internatl. Soc. Blood Transfusion. 1986; 515
   Google Scholar
• Wilkinson T., Como P., Brock P., Kronenberg H., Trent R. J. A., Brennan S. O. Hemoglobin I High Wycombe in an Australian family. Hemoglobin 1987; 11: 51
   PubMed Web of Science ®Google Scholar
• Dahmane‐Arbane M., Blouquit Y., Arous N., Bardakdjian J., Benamani M., Riou J., Benabadji M., Rosa J., Galacteros F. Hb Boumerdès α237 (C2)ProArgβ2: a new variant in an a chain associated with Hb S in an Algerian family (in French). Nouv. Rev. Fr. d'Hematol 1987; 29: 317
   PubMedGoogle Scholar
• Baklouti F., Giraud Y., Francina A., Richard G., Perier C., Geyssant A., Jaubert J., Brizard C., Delaunay J. Hemoglobin Grange‐Blanche ‘β27(B9) AlaVal’, a new variant with normal expression and increased affinity for oxygen. FEBS Lett 1987; 223: 59
   PubMed Web of Science ®Google Scholar
• Wada Y., Ikkala E., Imai K., Matsuo T., Matsuda H., Lehtinen M., Hayashi A., Lehmann H. Structure and function of a new hemoglobin variant, Hb Meilahti α2β236(C2)ProThr), characterized by mass spectrometry. Acta Haematol 1987; 78: 109
   PubMed Web of Science ®Google Scholar
• Zeng Y. T., Ren Z. R., Chen M. J., Zhao J. Q., Qiu X. K., Huang S. Z. A new unstable haemoglobin variant: Hb Shanghai ‘β131 (H9) GlnPro’ found in China. Br. J. Haematol 1987; 67: 221
   PubMed Web of Science ®Google Scholar
• Gilbert A. T., Fleming P. J., Sumner D. R., Hughes W. G., Ip F., Kwan Y. L., Holland R. A. B. Hemoglobin Randwick or β15(A12) TrpGly: A new unstable β‐chain hemoglobin variant. Hemoglobin 1988; 12: 149
   PubMed Web of Science ®Google Scholar
• Mrad A., Blouquit Y., Lacombe C., Blibech R., Arous N., Bardakdjian J., Kastally R., Rosa J., Galacteros F. Hb Tunis ‘α2β2124(H2)ProSer’. a new β chain variant identified by HPLC. Hemoglobin 1988; 12: 23
   PubMed Web of Science ®Google Scholar
• De Pablos J. Ma., Kutlar A., Wilson J. B., Webber B. B., Hu H., Huisman T. H. J. Hb D‐Granada or α2β222(B4)GluVal. Hemoglobin 1987; 11: 563
   PubMed Web of Science ®Google Scholar
• Baklouti F., Giraud Y., Francina A., Richard G., Favre‐Gilly J., Delaunay J. Hemoglobin Pierre‐Benite ‘β90(F6)GluAsp’, a new high affinity variant found in a French family. Hemoglobin 1988; 12: 171
   PubMed Web of Science ®Google Scholar
• Altay C., Gurgey A., Wilson J. B., Hu H., Webber B. B., Kutlar F., Huisman T. H. J. Hb F‐Baskent or α2Aγ128(H6)AlaThr. Hemoglobin 1988; 12: 87
   PubMed Web of Science ®Google Scholar
• Malcorra‐Azpiazu J. J., Balda‐Aguirre M. I., Diaz‐Chico J. C., Hu H., Wilson J. B., Webber B. B., Kutlar F., Kutlar A., Huisman T. H. J. Hb Las Palmas or α2β2 49(CD8)SerPhe, a mildly unstable hemoglobin variant. Hemoglobin 1988; 12: 163
   PubMed Web of Science ®Google Scholar
• Baudin‐Chich V., Wajcman H., Gombaud‐Saintonge G., Arous N., Riou J., Briere J., Galacteros F. Hemoglobin Brest ‘β127(H5) GinLys’ a new unstable human hemoglobin variant located at the α1β1 interface with specific electrophoretic behavior. Hemoglobin 1988; 12: 179
   PubMed Web of Science ®Google Scholar
• Ali M. A. M., Pinkerton P., Chow S. W. S., Zaetz S. D., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H. J. Some rare hemoglobin variants with altered oxygen affinity; Hb Linkoping ‘β36(C2)ProThr’, Hb Caribbean ‘β91(F7) LeuArg’, and Hb Sunnybrook ‘β36(C2) ProArg’. Hemoglobin 1988; 12: 137
   PubMed Web of Science ®Google Scholar
• Jogessar V. B., Westermeyer K., Webber B. B., Wilson J. B., Hu H., Gonzalez‐Redondo J. M., Kutlar A., Huisman T. H. J. Hb Natal or α2(minus Tyr‐Arg)β2, a high oxygen affinity α chain variant with a deleted carboxy‐terminus resulting from a TAC‐VTAA (Tyrterminating codon) mutation in codon α140. Biochim. Biophys. Acta 1988; 951: 36
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Imai N., Ueda S., Seki M. An electrophoretically silent hemoglobin variant, Hb Hekinan ‘α27(B8) GluAsp’ found in a Japanese. Hemoglobin 1988; 12: 61
   PubMed Web of Science ®Google Scholar
• Malcorra‐Azpiazu J. J., Balda‐Aguirre M. I., Diaz‐Chico J. C., Kutlar F., Kutlar A., Wilson J. B., Hu H., Huisman T. H. J. Hb Le Lamentin or α220(B1)HisGlnγ2 found in a Spanish family. Hemoglobin 1988; 12: 201
   PubMed Web of Science ®Google Scholar
• Wajcman H., Blouquit Y., Gombaud‐Saintonge G., Riou J., Galacteros F. Hemoglobin Fontainebleau ‘α21(B2)AlaPro’, a new silent mutant hemoglobin. Hemoglobin 1989; 13: 421
   PubMed Web of Science ®Google Scholar
• Wacjman J., Gombaud‐Saintonge G., Galacteros F., Martha M., Vertongen F. Hb Belliard ‘α56(E5)LysAsn’ a new fast‐moving α chain variant found in a subject of Spanish origin. Hemoglobin 1989; 13: 157
   PubMed Web of Science ®Google Scholar
• Gonzalez‐Redondo J. M., Wilson J. B., Kutlar A., Huisman T. H. J., Sicilia A., Romero C., Fernandes Fuertes I. Hb J‐Pontoise or α263(E12)AlaAspβ2 in four members of a Spanish family. Hemoglobin 1987; 11: 47
   PubMed Web of Science ®Google Scholar
• Bardakdjian‐Michau J., Lacombe C., Blouquit Y., Craescu C. T., Galacteros F., Lena‐Russo D., Orsini A., Vovan L. Hemoglobin N‐Timone ‘α2β28 (A5)LysGlu’: A new fast‐moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743
   PubMed Web of Science ®Google Scholar
• Gilbert A. T., Fleming P. J., Sumner D. R., Hughes W. G., Holland R. A. B., Tibben E. A. Hemoglobin Windsor or β11 (A8)ValAsp: A new unstable β‐chain hemoglobin variant producing a hemolytic anemia. Hemoglobin 1989; 13: 437
   PubMed Web of Science ®Google Scholar
• Gonzalez‐Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., Hu H., Wilson J. B., Huisman T. H. J. Hb Monroe or α2β230(B12)ArgThr, a variant associated with β‐thalassemia due to a GC substitution adjacent to the donor splice site of the first intron. Hemoglobin 1989; 13: 67
   PubMed Web of Science ®Google Scholar
• Honig G. R., Telfer M. C., Rosenblum B. B., Vida L. N. Hb Warsaw (β42 PheVal): An unstable hemoglobin with decreased oxygen affinity. I. Hematologic and clinical expression. Am. J. Hematol 1989; 32: 36
   PubMed Web of Science ®Google Scholar
• Bernini L. F., Giordano P. C. Hemoglobin Tilburg: α2β273 (E17) AspGly. A new hemoglobin with reduced oxygen affinity. Biochim. Biophys. Acta 1988; 957: 281
   PubMed Web of Science ®Google Scholar
• Hidaka K., Iuchi I., Miyake K., Nakahara H., Iwakawa G. Hb Fukuyama ‘β77(EF 1)HisTyr’: A new abnormal hemoglobin discovered in a Japanese. Hemoglobin 1988; 12: 391
   PubMed Web of Science ®Google Scholar
• Bardakdjian J., Kister J., Rhoda M. D., Marden M., Arous N., De Leon J., North M. L., Lacombe C., Blouquit Y., Castracane C., Riou J., Rosa J., Galacteros F. Hb J‐Cordoba ‘α2Aβ295(FG2) LysMet’ a new Hb variant found in Argentina. Hemoglobin 1988; 12: 1
   PubMed Web of Science ®Google Scholar
• Ohba Y., Imai K., Kumada I., Ohsawa A., Miyaji T. Hb Mori‐guchi or α2β297(FG4)HisTyr substitution at the α1β2 interface. Hemoglobin 1989; 13: 367
   PubMed Web of Science ®Google Scholar
• Kobayashi Y., Fukumaki Y., Komatsu N., Ohba Y., Miyaji T., Miura Y. A novel globin structural mutant, Showa‐Yakushiji (β110 Leu‐Pro) causing a β‐thalassemia phenotype. Blood 1987; 70: 1688
   PubMed Web of Science ®Google Scholar
• Blanke S., Johnsen A., Wimberley P. D., Mortensen H. B. Hemoglobin Hafhia: α(β116 (G18) HisGln)2; a new hemoglobin variant mistaken for glycated hemoglobin. Biochim. Biophys. Acta 1988; 955: 214
   PubMed Web of Science ®Google Scholar
• Keclard L., Campier A., Merault G., Auperin A., Riou J., Rosa J., Galacteros F. Hemoglobin Nevers ‘α2β2130(H8)TyrSer’ a new silent variant found in France. Hemoglobin 1990; 14: 103
   PubMed Web of Science ®Google Scholar
• Villegas A., Martin G., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H. J. Hb Extremadura or α2β2133(H11) ValLeu, a mildly unstable hemoglobin in a Spanish female. Hemoglobin 1989; 13: 505
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. L., Johnson M. H., Olsen K. W., Shih D., Jones R. T., Lux S. E., Rodgers P., Arnone A. Hemoglobin Brockton ‘β138(H16) AlaPro’: An unstable variant near the C‐terminus of the β‐subunits with normal oxygen‐binding properties. Biochemistry 1988; 27: 7614
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Johnson M. H., Jue D. L., Lonser R. Hemoglobin Hinsdale ‘β139(H17)AsnLys’: A variant in the central cavity showing reduced affinity for oxygen and 2,3‐diphosphoglycerate. Hemoglobin 1989; 13: 455
   PubMed Web of Science ®Google Scholar
• de Pablos J. Ma., Clegg J. B. Hb F‐Granada or α2γ222(B4m) AspVal: A new human fetal hemoglobin variant. Hemoglobin 1988; 12: 405
   PubMed Web of Science ®Google Scholar
• Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Hu H., Huisman T. H. J. Hb F‐Austell or α2Gγ2240(C6)ArgLys. Hemoglobin 1988; 12: 409
   PubMed Web of Science ®Google Scholar
• Hidaka K., Iuchi I., Nakahara H., Iwakawa C. Hb F‐Fukuyama or AγT43 (CD2)AspAsn. Hemoglobin 1989; 13: 93
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Bardakdjian J., Lena‐Russo D., Arous N., Perrimond H., Orsini A., Rosa J., Galacteros F. Hemoglobin Bruxelles: α2Aβ241 or 42 (C7 or CD1) Phedeleted. Hemoglobin 1989; 13: 465
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Swan D. C., Hine T. K., Baine R. M., Jue D. L., Benson J. M., Johnson M. H., Virshup D. M., Zinkham W. H. Hb Catonsville (glutamic acid inserted between Pro‐37(C2)α and Thr‐38(C3)α) ‐ Nonallelic gene conversion in the globin system?. J. Biol. Chem 1989; 264: 21454
   PubMed Web of Science ®Google Scholar
• Kawata R., Ohba Y., Yamamoto K., Miyaji T., Makita R., Ohga K., Watanabe S., Miwa S. Hyperunstable Hemoglobin Koriyama anti‐Hb Gun Hill insertion of five residues in the β chain. Hemoglobin 1988; 12: 311
   PubMed Web of Science ®Google Scholar
• Delanoe‐Garin J., Blouquit Y., Arous N., Kister J., Poyart C., North M. L., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Saverne: A new variant with elongated β chains: Structural and functional properties. Hemoglobin 1988; 12: 337
   PubMed Web of Science ®Google Scholar
• Gale R. E., Blair N. E., Huehns E. R., Clegg J. B. Hb A‐like sickle haemoglobin: Hb S‐Providence. Br. J. Haematol 1988; 70: 251
   PubMed Web of Science ®Google Scholar
• Langdown J. V., Williamson D., Knight C. B., Rubenstein D., Carrell R. W. Case Report ‐ A new doubly substituted sickling haemoglobin: HbS‐Oman. Br. J. Haematol 1989; 71: 443
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Williamson D., Symmans W. A., Carrell R. W. Two de novo mutations in one β globin chain: Hemoglobin Atlanta‐Coventry, β75 LeuPro and (β141 Leu‐Kleleted. Hemoglobin 1986; 10: 225
   PubMed Web of Science ®Google Scholar
• Ahmad A., Naqvi S., Ehsanullah S., Zaidi Z. H. Abnormal hemoglobins11 = Hb (Karachi), an a chain abnormality at position δ AlaPro. J. Pakistani Med. Assoc 1986; 36: 206
   PubMedGoogle Scholar
• Codrington J. F., Codrington F. A., Wisse J. H., Wilson J. B., Webber B. B., Wong S. C., Huisman T. H. J. Hb Chad or α223(B4)GluLysβ2 observed in members of a Surinam family in association with α‐thalasse‐mia‐2 and with Hb S. Hemoglobin 1989; 13: 543
   PubMed Web of Science ®Google Scholar
• Bardakdjian‐Michau J., Rosa J., Galacteros F., Lancelot M., Marquart F. X. Hb Reims ‘α223(B4)GluGlyβ2’: A new a chain variant with slightly decreased stability. Hemoglobin 1989; 13: 733
   PubMed Web of Science ®Google Scholar
• Groff P., Galacteros F., Kalmes G., Blouquit Y., Wajcman H. Hb Luxembourg ‘α24(B5)TyrHis’: A new unstable variant. Hemoglobin 1989; 13: 429
   PubMed Web of Science ®Google Scholar
• Ohba Y., Imai K., Uenaka R., Ami M., Fujisawa K., Itoh K., Hira‐kawa K., Miyaji T. Hb Miyano or α41(C6)ThrSer: A new high oxygen affinity a chain variant found in an erythremic blood donor. Hemoglobin 1989; 13: 637
   PubMed Web of Science ®Google Scholar
• Giordano P. C., Fodde R., Amons R., Ploem J. E., Bernini L. F. Hemoglobin J‐Anatolia ‘α61(E10)LysThr’: Structural characterization and gene localization of a new a chain variant. Hemoglobin 1990; 14: 119
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Webber B. B., Kutlar A., Reese A. L., McKie V. C., Lutcher C. L., Felice A. E., Huisman T. H. J. Hb Evans or α262 (El 1)ValMetβ2; an unstable hemoglobin causing a mild hemolytic anemia. Hemoglobin 1989; 13: 557
   PubMed Web of Science ®Google Scholar
• Baklouti F., Baudin‐Chich V., Kister J., Marden M., Teyssier G., Poyart C., Delaunay J., Wajcman H. Increased oxygen affinity with normal heterotropic effects in hemoglobin Loire ‘α88(F9)AlaSer’. Eur. J. Biochem 1988; 177: 307
   PubMedGoogle Scholar
• Wajcman H., Delaunay J., Francina A., Rosa J., Galacteros F. Hemoglobin Nouakchott ‘α114(GH2)ProLeu’: A new hemoglobin variant displaying an unusual increase in hydrophobicity. Biochim. Biophys. Acta 1989; 998: 25
   PubMed Web of Science ®Google Scholar
• Harkness M., Harkness D. R., Kutlar F., Kutlar A., Wilson J. B., Webber B. B., Codrington J. F., Huisman T. H. J. Hb Sun Prairie or α2130(H13)AlaProβ2, a new unstable variant occurring in low quantities. Hemoglobin 1990; 14: 479
   PubMed Web of Science ®Google Scholar
• McDonald M. J., Michalski L. A., Turci S. M., Guillette R. A., Jue D. L., Johnson M. H., Moo‐Penn W. F. Structural, functional, and sub‐unit assembly properties of Hemoglobin Attleboro ‘α138 (H21) Ser Pro’, a variant possessing a site mutation at a critical C‐terminal residue. Biochemistry 1990; 29: 173
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Imai K., Ohkuma A., Koya Y., Takahashi H. Hb Fukuoka ‘β2(NA2)HisTyr’: A new abnormal hemoglobin with a substituted amino acid at the 2,3‐diphosphoglycerate binding site. Hemoglobin 1990; 14: 199
   PubMed Web of Science ®Google Scholar
• Yang K. G., Kutlar F., George E., Wilson J. B., Kutlar A., Stoming T. A., Gonzalez‐Redondo J. M., Huisman T. H. J. Molecular characterization of β‐globin gene mutations in Malay patients with Hb E‐β‐thalassaemia and thalassaemia major. Br. J. Haematol 1989; 72: 73
   PubMed Web of Science ®Google Scholar
• Vidaud M., Gattoni R., Stevenin J., Vidaud D., Amselem S., Chibani J., Rosa J., Goossens M. A 5′ splice‐region GC mutation in exon 1 of the human β‐globin gene inhibits pre‐mRNA splicing: A mechanism for β+‐thalassemia. Proc. Natl. Acad. Sci. USA 1989; 86: 1041
   PubMed Web of Science ®Google Scholar
• Li H. J., Zhao X. N., Li H. W., Liang K. X., Wang R. P., Chang T. T., Wilson J. B., Webber B. B., Huisman T. H. J. A new slow‐moving hemoglobin variant Hb Tianshui or aLβ239(C5)GlnArg, observed in a Chinese family living in Gansu. Hemoglobin 1990; 14: 569
   PubMed Web of Science ®Google Scholar
• Honig G. R., Vida L. N., Rosenblum B. B., Perutz M. F., Fermi G. Hemoglobin Warsaw ‘pheβ42(CD1)Val’, an unstable variant with decreased oxygen affinity ‐ Characterization of its synthesis, functional properties, and structure. J. Biol. Chem 1990; 265: 126
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Webber B. B., Kutlar A., Huisman T. H. J. Hb Gainesville‐GA, or
   Google Scholar
• Sciarratta G. V., Ivaldi G. Hb Matera ‘α55(D6)MetLys’: A new unstable hemoglobin variant in an Italian family. Hemoglobin 1990; 14: 79
   PubMed Web of Science ®Google Scholar
• Williamson D., Nutkins J., Rosthoj S., Brennan S. O., Carrell R. W. Characterization of Hb Aalborg, a new unstable hemoglobin variant, by fast atom bombardment mass spectrometry. Hemoglobin 1990; 14: 137
   PubMed Web of Science ®Google Scholar
• Dash S., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H. J. Hb Chandigarh or α2β294(FG1)AspGly observed in an Indian family. Hemoglobin 1989; 13: 749
   PubMed Web of Science ®Google Scholar
• Jones R. T., Saointz H. I., Head C., Shih D. T. B., Fairbanks V. F. Hb Johnstown ‘β109(G11)ValLeu’: A new electrophoretically silent variant that causes erythrocytosis. Hemoglobin 1990; 14: 147
   PubMed Web of Science ®Google Scholar
• Wajcman H., Mrad A., Blouquit Y., Parmentier C., Riou J., Galacteros F. Hemoglobin Villejuif ‘β123(H1) ThrIle’: A new variant found in coincidence with polycythemia vera. Am. J. Hematol 1989; 32: 294
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Imai K., Marubashi S. Hb Yamagata ‘β132(H10)LysAsn’: A new abnormal hemoglobin in a Japanese family. Hemoglobin 1990; 14: 207
   PubMed Web of Science ®Google Scholar
• Ulukutlu L., Ozsahin H., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H. J. Hb Brockton
   Google Scholar
• Martins M. C., Rosado L., Wilson J. B., Kutlar A., Hu H., Huisman T. H. J. Hb Himeji or α2β2140(H18)AlaAsp in a Portuguese family. Hemoglobin 1989; 13: 411
   PubMed Web of Science ®Google Scholar
• Plaseska D., Li H. ‐J., Wilson J. B., Kutlar F., Kutlar A., Huisman T. H. J., Kulpa J. Hb F‐Brooklyn or α2Gγ266(E10)LysGln. Hemoglobin 1990; 14: 213
   PubMed Web of Science ®Google Scholar
• Priest J. R., Watterson J., Jones R. T., Faassen A. E., Hedlund B. E. Mutant fetal hemoglobin causing cyanosis in a newborn. Pediatrics 1989; 83: 734
   PubMed Web of Science ®Google Scholar
• Glader B. E. Hemoglobin FM‐Fort Ripley: Another lesson from the neonate. Pediatrics 1989; 83: 792
   PubMed Web of Science ®Google Scholar
• Plaseska D., Kutlar F., Wilson J. B., Webber B. B., Zeng Y. ‐T., Huisman T. H. J. Hb F‐Jiangsu, the first γ chain variant with a valine methionine substitution: α2Aγ2134(H12)ValMet. Hemoglobin 1990; 14: 177
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Doi K., Ueda S., Imai K., Ohba Y., Kutlar F., Huisman T. H. J. Hb F‐Onoda or α2Gγ2146(HC3)BisTyr, a newly discovered fetal hemoglobin variant in a Japanese newborn. Hemoglobin 1990; 14: 217
   PubMed Web of Science ®Google Scholar
• Codrington J. F., Kutlar F., Harris H. F., Wilson J. B., Stoming T. A., Huisman T. H. J. Hb A2‐Wrens or α2δ298 (FG5)ValMet, an unstable δ chain variant identified by sequence analysis of amplified DNA. Biochim. Biophys. Acta 1989; 1009: 87
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Codrington J. F., Prchal J. T., Hall K. M., de Pablos J. Ma., Rodriguez I., Huisman T. H. J. Hb Birmingham and Hb Galicia: Two unstable β chain variants characterized by small deletions and insertions. Blood 1990; 75: 1883
   PubMed Web of Science ®Google Scholar
• Ohba Y., Ami M., Imai K., Komatsu K., Amatsu K. Hb Masuda ‘β114(G16)LeuMet, 119(GH2)GlyAsp’, a hemoglobin with two substitutions in the β chain. Hemoglobin 1989; 13: 753
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Webber B. B., Plaseska D., de Alarcon P. A., McMillan S. K., Huisman T. H. J. Hb Davenport or α278(EF7)AsnHisβ2. Hemoglobin 1990; 14: 599
   PubMed Web of Science ®Google Scholar
• Ohba Y., Fujisawa K., Imai K., Leowattana W., Tani Y., Ami M., Miyaji T. A new a chain variant Hb Tonosho ‘α1 10(G17)AlaThr’: Subunit dissociation during cation exchange chromatography for Hb AIc assay. Hemoglobin 1990; 14: 413
   PubMed Web of Science ®Google Scholar
• Hidaka K., Iuchi I., Kobayashi T., Katoh K., Yaguchi K. Hb Fukutomi ‘α126 (H9)AspVaTJ: A new hemoglobin variant with high oxygen affinity. Hemoglobin 1990; 14: 499
   PubMed Web of Science ®Google Scholar
• Plaseska D., Gu L. ‐H., Wilson J. B., Codrington J. F., Huisman T. H. J., Dash S. Hb Sun Prairie or α2130(H13)AlaProβ2; second observation in an Indian adult. Hemoglobin 1990; 14: 491
   PubMed Web of Science ®Google Scholar
• Wajcman H., Vasseur C., Blouquit Y., Rosa J., Labie D., Najman A., Reman O., Leporrier M., Galacteros F. Unstable alpha‐chain hemoglobin variants with factitius beta‐thalassemia biosynthetic ratio: Hb Questembert (α131‘H14’ SerPro) and Hb Caen (α132 ‘H15’ValGly). Am. J. Hematol 1993; 42: 367
   PubMed Web of Science ®Google Scholar
• Wajcman H., Blouquit Y., Riou J., Kister J., Poyart C., Soria J., Galacteros F. A new hemoglobin variant found during investigations of diabetes mellitus: Hb Pavie‘α135(H18)ValGlu’. Clin. Chim. Acta 1990; 188: 39
   PubMed Web of Science ®Google Scholar
• Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K. A new hemoglobin variant, Hb Hanamaki or α2139(HC1)GlyGluβ2, found in a Japanese family. Hemoglobin 1992; 16: 67
   PubMed Web of Science ®Google Scholar
• Lena‐Russo D., Orsini A., Vovan L., Bardakdjian‐Michau J., Lacombe C., Blouquit Y., Craescu C. T., Galacteros F. Hb N‐Timone ‘α2β28(A5)LysGlu’: A new fast‐moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743
   PubMed Web of Science ®Google Scholar
• Spivak V. A. Letter to the Editor. Hemoglobin 1989; 13: 219–220
   PubMedGoogle Scholar
• Gaudry C. L., Jr., Pitel P. A., Jue D. L., Hine T. K., Johnson M. H., Moo‐Penn W. F. Hb Jacksonville ‘α2β254(D5)ValAsp’: A new unstable variant found in a patient with hemolytic anemia. Hemoglobin 1990; 14: 653
   PubMed Web of Science ®Google Scholar
• Podda A., Galanello R., Maccioni L., Melis M. A., Rosatelli C., Perseu L., Cao A. Hemoglobin Cagliari (β60‘E4’ValGlu): A novel unstable thalassemic hemoglobinopathy. Blood 1991; 77: 371
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Marden M., Bonn B., Blouqut Y., Descamps J., Goudemand M., Poyart C., Galacteros F. Hemoglobin Calais ‘β76(E20) AlaPro’: A hemoglobin variant with decreased intrinsic oxygen affinity. Biochim. Biophys. Acta 1991; 1096: 60
   Web of Science ®Google Scholar
• Witkowska H. E., Lubin B. H., Beuzard Y., Baruchel S., Esseltine D. W., Vichinsky E. P., Kleman K. M., Bardakdjian‐Michau J., Pinkoski L., Cahn S., Rottman E., Green B. N., Falick A. M., Shackleton C. H. L. Sickle cell disease in a patient with sickle cell trait and compound heterozygosity for Hemoglobin S and Hemoglobin Quebec‐Chori. N. Engl. J. Med 1990; 325: 1150
   Web of Science ®Google Scholar
• Kutlar F., Felice A. E., Grech J. L., Bannister W. H., Kutlar A., Wilson J. B., Webber B. B., Hu H., Huisman T. H. J. The linkage of Hb Valletta ‘α2β287 (F3)ThrPro’ and Hb F‐Malta‐I ‘α2Gγ2117(G19)HisArg’ in the Maltese population. Hum. Genet 1991; 86: 591
   PubMed Web of Science ®Google Scholar
• Wajcman H., Vasseur C., Blouquit Y., Esperito Santo D., Peres M. J., Martins M. C., Poyart C., Galacteros F. Hemoglobin Redondo ‘β92(F8)HisAsn’: An unstable hemoglobin variant associated with heme loss which occurs in two forms. Am. J. Hematol 1991; 38: 194
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishi‐narita M. Hb Isehara (or Hb Redondo) ‘β92(F8)HisAsn’: An unstable variant with a proximal histidine substitution at the heme contact. Hemoglobin 1991; 15: 279
   PubMed Web of Science ®Google Scholar
• Honig G. R., Vida L. N., Latorraca R., Divgi A. B. Hb South Milwaukee ‘β105 (G7)LeuPhe’: A newly‐identified hemoglobin variant with high oxygen affinity. Am. J. Hematol 1990; 34: 199
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kushida Y., Ueda S. A new abnormal variant, Hb Yahata or β112(G14)CysTyr, found in a Japanese: Structural confirmation by DNA sequencing of the β‐globin gene. Hemoglobin 1991; 15: 109
   PubMed Web of Science ®Google Scholar
• Plaseska D., Wilson J. B., Gu L. ‐H., Kutlar F., Huisman T. H. J., Zeng Y. ‐T., Shen M. Hb Zengcheng or α2β2114(G16)LeuMet. Hemoglobin 1990; 14: 555
   PubMed Web of Science ®Google Scholar
• Plaseska D., de Alarcon P. A., McMillan S., Walbrecht M., Wilson J. B., Huisman T. H. J. Hb Iowa or α2β2119(GH2)GlyAla. Hemoglobin 1990; 14: 423
   PubMed Web of Science ®Google Scholar
• Abourzik N. N., Conlon M., Zordon G., Hine T. K., Johnson M. H., Jue D. L., Moo‐Penn W. F. Hb St. Francis ‘β 121 (GH4)GluGly’: A new mutation at the same site as Hb D‐Los Angeles. Hemoglobin 1991; 15: 115
   PubMed Web of Science ®Google Scholar
• Bardakdjian‐Michau J., Fucharoen S., Delanoe‐Garin J., Kister J., Lacombe C., Wini‐chagoon P., Blouquit Y., Riou J., Wasi P., Galacteros F. Hemoglobin Dhonburi α2β2126(H4)ValGly: A new unstable β variant producing β‐thalassemia intermedia phenotype in association with βd`‐thalassemia. Am. J. Hematol 1990; 35: 96
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kushida Y., Ueda S. Structural analysis of abnormal hemoglobin by the polymerase chain reaction. Jap. J. Clin. Pathol 1990; 38: 1067
   PubMedGoogle Scholar
• Plaseska D., Wilson J. B., Kutlar F., Font L. I., Baiget M., Huisman T. H. J. HbF‐Catalonia or α2Gγ215(A12)TrpArg. Hemoglobin 1990; 14: 511
   PubMed Web of Science ®Google Scholar
• Qualtieri A., Crescibene L., Bagala A., De Marco E. V., Bria M., Brancati C. Hb F‐Cosenza or Gγ25(B7)GlyGlu: A new fast‐moving fetal hemoglobin variant. Hemoglobin 1991; 15: 509
   PubMed Web of Science ®Google Scholar
• Huisman T. H. J., Kutlar F., Gu L. ‐H. γ Chain abnormalities and y‐globin gene rearrangements in newborn babies of various populations. Hemoglobin 1991; 15: 393
   PubMed Web of Science ®Google Scholar
• Plaseska D., Kutlar F., Wilson J. B., Fei Y. J., Huisman T. H. J. Hb F‐Charlotte, an Aγ variant with a threonine residue in position γ75 and a glycine residue in position γ136. Hemoglobin 1990; 14: 617
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kushida Y., Ueda S., Kawakami H. Hb A2‐Niigata ‘δ1(NA1)ValAla’: A new δ chain variant found in the Japanese population. Hemoglobin 1991; 15: 335
   PubMed Web of Science ®Google Scholar
• Leung H., Gilbert A. T., Fleming P. J., Wong J., Hughes W. G., Hussein S., Nash A. R. Hb A2‐Parkville or δ47(CD6)AspVal: A new δ chain variant. Hemoglobin 1991; 15: 407
   PubMed Web of Science ®Google Scholar
• Plaseska D., Dimovski A. J., Wilson J. B., Webber B. B., Hume H. A., Huisman T. H. J. Hemoglobin Montreal, a new variant with an extended β chain due to a deletion of Asp, Gly, Leu at positions 73, 74, and 75, and in insertion of Ala, Arg, Cys, Gin at the same location. Blood 1991; 77: 178
   PubMed Web of Science ®Google Scholar
• Vasseur C., Guillemin C., Galacteros F., Wajcman H. Hemoglobin Thionville: An alpha chain variant with substitution of a glutamic residue for valine NA‐1 and having an extended N‐terminus. Blood 1990; 76(Suppl. 1)78a
   Google Scholar
• Lacombe C., Prome D., Blouquit Y., Bardakdjian J., Arous N., Mrad A., Prome J. ‐C., Rosa J. New results of hemoglobin variant structure determinations by fast atom bombardment mass spectrometry. Hemoglobin 1990; 14: 529
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Ramachandran M., Webber B. B., Kutlar F., Hazelwood L. F., Barnett D., Hirschler N. V., Huisman T. H. J. Hb Cleveland or α2β293(F9)CysArg; 121(GH4)GluGln. Hemoglobin 1991; 15: 269
   PubMed Web of Science ®Google Scholar
• Coleman M. B., Steinberg M. H., Adams J. G., III. Hemoglobin Terre Haute arginine β106. A posthumous correction to the original structure of Hemoglobin Indianapolis. J. Biol. Chem 1991; 266: 5798
   PubMed Web of Science ®Google Scholar
• Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K., Imai K. Hb Kanagawa ‘α40(C5)LysMet’: A new a chain variant with an increased oxygen affinity. Hemoglobin 1992; 16: 1
   PubMed Web of Science ®Google Scholar
• Zwerdling T., Williams S., Nasr S. A., Rucknagel D. L. Hb Port Huron ‘α56(E5)LysArg’: A new α chain variant. Hemoglobin 1991; 15: 381
   PubMed Web of Science ®Google Scholar
• Perry M. C., Head C., Fairbanks V. F., Jones R. T., Taylor H., Proud V. Hemoglobin Columbia Missouri or α2‘88(F9)AlaVaT’β2: A new high‐oxygen‐affinity hemoglobin that causes erythrocytosis. Mayo Clin. Proc 1991; 66: 5
   PubMed Web of Science ®Google Scholar
• Langdown J. V., Davidson R. J. L., Williamson D. A new a chain variant, Hb Turriff ‘α99(G6)LysGlu’: The interference of abnormal hemoglobins in Hb A1c determination. Hemoglobin 1992; 16: 11
   PubMed Web of Science ®Google Scholar
• Fujisawa K., Hattori Y., Ohba Y., Ando S. Hb Yuda or α130 (H13)AlaAsp: A new a chain variant with low oxygen affinity. Hemoglobin 1992; 16: 435
   PubMed Web of Science ®Google Scholar
• Thein S. L., Best S., Sharpe J., Paul B., Clark D. J., Brown M. J. Hemoglobin Chesterfield (β28 LeuArg) produces the phenotype of inclusion body β thalassemia. Blood 1991; 77: 2791
   PubMed Web of Science ®Google Scholar
• Ramachandran M., Gu L. ‐H., Wilson J. B., Kitundu M. N., Adekile A. D., Liu J. ‐C., McKie K. M., Huisman T. H. J. Hb Muscat or α2β232(B14)LeuVal observed in an Arabian family in association with Hb S. Hemoglobin 1992; 16: 259
   PubMed Web of Science ®Google Scholar
• Molchanova T. P., Wilson J. B., Gu L. ‐H., Guemira F., Fattoum S., Huisman T. H. J. Hb Bab‐Saadoun or α2β248(CD7)LeuPro, a mildly unstable variant found in an Arabian boy from Tunisia. Hemoglobin 1992; 16: 267
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J. C., Cottenceau D., Galacteros F. Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: The example of Hb La Roche‐Sur‐Yon ‘β81(EF5)LeuHis’. Biochim. Biophys. Acta 1992; 1138: 127
   PubMed Web of Science ®Google Scholar
• Tamagnini G. P., Ribeiro M. L., Valente V., Ramachandran M., Wilson J. B., Baysal E., Gu L. ‐H., Huisman T. H. J. Hb Coimbra or α2β299(G1)AspGlu, a newly discovered high oxygen affinity variant. Hemoglobin 1991; 15: 487
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Vasseur C., Blouquit Y., Behnken J. L., Galacteros F. Hb Ingelheim ‘β99(G1)AspGlu’: A new high affinity hemoglobin variant destabilizing the α1β2 interrace. Blood 1991; 78(Suppl. 1)206a
   Google Scholar
• Como P. F., Wylie B. R., Trent R. J., Bruce D., Volpato F., Wilkinson T., Kronenberg H., Holland R. A. B., Tibben E. A. A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore ‘β111 (G13)ValAla’. Hemoglobin 1991; 15: 53
   PubMed Web of Science ®Google Scholar
• Pagano L., Lacerra G., Camardella L., De Angioletti M., Fioretti G., Maglione G., de Bonis C., Guarino E., Viola A., Cutolo R., De Rosa L., Carestia C. Hemoglobin Neapolis, β126(H4)ValGly: A novel β‐chain variant associated with a mild β‐thalassemia phenotype and displaying anomalous stability features. Blood 1991; 78: 3070
   PubMed Web of Science ®Google Scholar
• Duwig I., North M. L., Barth J. G., Rieffel M., Nierengarten P., Arous N., Riou J., Galacteros F. Aspects hematologiques et anomalies structurales d'une nouvelle hemoglobine instable: L'Hb Sarrebourg β131(H9)GlnArg. Abstract. Nouv. Rev. Fr. d'Hematol 1987; 29: 344
   Google Scholar
• Rahbar S., Lee T., Asmeron Y. Hb Beckman α2β2135(H13) AlaGlu: A new unstable variant and reduced oxygen affinity. Blood 1991; 78(Suppl. 1)204a
   Google Scholar
• Como P. F., Hocking D. R., Swinton G. W., Trent R. J., Holland R. A. B., Tibben E. A., Wilkinson T., Kronenberg H. Hb Geelong ‘β139(H17)AsnAsp’. Hemoglobin 1991; 15: 85
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Hine T. K., Johnson M. H., Jue D. L., Holland S., George S., Pierce A. M., Michalski L. A., McDonald M. J. Hb Rancho Mirage ‘β143(H21)HisAsp’; a variant in the 2,3‐DPG binding site showing normal oxygen affinity at physiological pH. Hemoglobin 1992; 16: 35
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., Matsunaga T. Hb Kodaira ‘β146(HC3)HisGln’: A new β chain variant with an amino acid substitution at the C‐terminus. Hemoglobin 1992; 16: 85
   PubMed Web of Science ®Google Scholar
• Wajcman H., Blouquit Y., Vasseur C., Le Querrec A., Melevendi C., Rasore A., Galacteros F. Two new human hemoglobin variants caused by unusual mutational events: Hb Zaïre contains a five residue repetition within the α‐chain and Hb Duino has two residues substituted in the β‐chain. Hum. Genet 1992; 78: 676
   Web of Science ®Google Scholar
• Trifillis P., Ioannou P., Schwartz E., Surrey S. Identification of four novel δ‐globin gene mutations in Greek Cypriots using polymerase chain reaction and automated fluorescence‐based DNA sequence analysis. Blood 1991; 78: 3298
   PubMed Web of Science ®Google Scholar
• Abbes S., M'Rad A., Fitzgerald P. A., Dormer P., Blouquit Y., Kister J., Galacteros F., Wajcman H. Hb A1‐Ain Abu Dhabi ‘α18(A16) GlyAsp’: A new hemoglobin variant discovered in an Emiratee family. Hemoglobin 1992; 16: 355
   PubMed Web of Science ®Google Scholar
• Cürük M. A., Dimovski A. J., Baysal E., Gu L. ‐H., Kutlar F., Molchanova T. P., Webber B. B., Altay C., Gürgey A., Huisman T. H. J. Hb Adana or α259 (E8)GlyAspβ2, a severely unstable α1‐globin variant, observed in combination with the ‐(α)20.5 kb α‐thal‐1 deletion in two Turkish patients. Am. J. Hematol 1993; 44: 270
   PubMed Web of Science ®Google Scholar
• Ferranti P., Palapiano A., Malorni A., Pucci P., Marino G., Cossu G., Manca L., Masala B. Hemoglobin Ozieri: A new α‐chain variant ‘α71(E20)AlaVal’. Characterization using FAB‐ and electrospray‐mass spectrometric techniques. Biochim. Biophys. Acta 1993; 1162: 203
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Galacteros F., Josifovska O., Spielvolgel A., Nagel R. L. Hb Montefiore ‘α126(H9)AspTyr’: An abnormal hemoglobin with high oxygen affinity and absence of cooperativity. Blood 1992; 80(Suppl. 1)82a
   Google Scholar
• Webber B. B., Wilson J. B., Gu L. ‐H., Huisman T. H. J. Hb Ethiopia or a 140 (HC2)TyrHisβ2. Hemoglobin 1992; 16: 441
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Marden M., Lahary A., Monconduit M., Galacteros F. Hemoglobin Rouen (α‐140 (HC2) TyrHis): alteration of the α‐chain C‐terminal region and moderate increase in oxygen affinity. Biochim. Biophys. Acta 1992; 1180: 53
   PubMed Web of Science ®Google Scholar
• Liu J. ‐S., Molchanova T. P., Gu L. ‐H., Wilson J. B., Hopmeier P., Schnedl W., Balaun E., Krejs G. J., Huisman T. H. J. Hb Graz or α2β22(NA2)HisLeu; a new β chain variant observed in four families from Southern Austria. Hemoglobin 1992; 16: 493
   PubMed Web of Science ®Google Scholar
• Divoky V., Bisse E., Wilson J. B., Gu L. ‐H., Wieland H., Heinrichs I., Prior J. F., Huisman T. H. J. Heterozygosity for the IVS‐I‐5 (GC) mutation with a GA change at codon 18 (ValMet; Hb Baden) in cis and a TG mutation at codon 126 (ValGly; Hb Dhonburi) in trans resulting in a thalassemia intermedia. Biochim. Biophys. Acta 1992; 1180: 173
   PubMed Web of Science ®Google Scholar
• Landin B. Hb Karlskoga or αP221(B3)AspHis, a new slow‐moving variant found in Sweden. Hemoglobin 1993; 17: 201
   PubMed Web of Science ®Google Scholar
• Ward C. M., Fay K. C., Brennan J., Lowrey I., Blacklock H. A. The use of the polymerase chain reaction in the identification of a high oxygen affinity haemoglobin ‐ Hb Finlandia. Aust. New Zeal. J. Med 1992; 22: 390
   PubMedGoogle Scholar
• Molchanova T. P., Postnikov Yu. V., Gu L. ‐H., Prior J. F., Raven J. L., Bennett J. A., Huisman T. H. J. Hb Tigraye or α2β279(EF3) AspHis(THE INDIA LIMITED COMPANYACĆC): A stable hemoglobin variant with increased oxygen affinity observed in an Ethiopian male. Hemoglobin 1993; 17: 247
   PubMed Web of Science ®Google Scholar
• Broxson E. H., Hine T. K., Moo‐Penn W. F. Hb Muskegon ‘β83 (EF7)GlyArg’: A new variant found in a family from the U. S. Hemoglobin 1993; 17: 85
   PubMed Web of Science ®Google Scholar
• deCastro C. M., Lee M., Fleenor D. E., Devlin B., Kaufman R. E. A novel β‐globin mutation, βDurham‐N. C. ‘β(114)LeuPro’, detected by SSCP, produces a dominant thalassemia‐like phenotype. Blood 1992; 80(Suppl. 1)6a
   Google Scholar
• Welch S., Bateman C. HbD‐Neath or β121(GH4)GluAla: Anew member of the Hb D family. Hemoglobin 1993; 17: 255
   PubMed Web of Science ®Google Scholar
• Molchanova T. P., Postnikov Yu. V., Gu L. ‐H., Huisman T. H. J. Hb A2‐Grovetown or α2δ275(E19)LeuVal. Hemoglobin 1993; 17: 289
   PubMed Web of Science ®Google Scholar
• Merritt D., Jones R. T., Head C., Shih D., Xiao H., Thibodeau S. N., Fairbanks V. F. Hb Seal Rock: An extended a chain variant associated with anemia microcytosis and α‐thalassemia‐2 (‐3.7 kb). Hemoglobin
   Google Scholar
• Brennan S. O., Shaw J., Allen J., George P. M. β141 Leu is not deleted in the unstable haemoglobin Atlanta‐Coventry but is replaced by a novel amino acid of mass 129 daltons. Br. J. Haematol 1992; 81: 99
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Shaw J. G., George P. M., Huisman T. H. J. Posttranslational modification of β141 Leu associated with the β75 (E19)LeuPro mutation in Hb Atlanta. Hemoglobin 1993; 17: 1
   PubMed Web of Science ®Google Scholar
• Hall G. W., Thein S. L., Newland A. C., Chisholm M., Traeger‐Synodinos, Higgs D. R. A novel mutation (T‐C) in codon 29 of the α2 globin gene produces a structural haemoglobin variant and a thalassaemia. Br. J. Haematol 1993; 84(Suppl. 1)63
   Google Scholar
• Bardakdjian J., Kister J., Wajcman H., Boulard P., Bonn B., Blouquit Y., Galacteros F. Hb Poitiers ‘α45(CE3)HisAsp’: A new hemoglobin variant with a two‐fold increase in oxygen affinity. Hemoglobin 1994; 18: 1
   PubMed Web of Science ®Google Scholar
• Giordano P. C., Harteveld C. L., Streng H., Oosterwijk J. C., Heister J. G. A. M., Amons R., Bernini L. F. Hb Kurdistan ‘α47(CE5)Asp Tyr’, a new a chain variant in combination with PβdG‐thalassemia. Hemoglobin 1994; 18: 11
   PubMed Web of Science ®Google Scholar
• Williamson D., Langdown J. V., Myles T., Mason C., Henthorn J. S., Davies S. C. Polycythaemia and microcytosis arising from the combination of a new high oxygen affinity haemoglobin (Hb Luton, α89 His Leu) and α thalassaemia trait. Br. J. Haematol 1992; 82: 621
   PubMed Web of Science ®Google Scholar
• Kister J., Soummer A. M., M'rad A., Bonn B., Prome D., Cappellino B., Chambon P., Wajcman H., Galacteros F. Hb Cemenelum ‘α92 (FG4) ArgTrp’: A hemoglobin variant with a moderately increased oxygen affinity. Abstract, Journees Scienti‐fiques du Club de L'Hemoglobin. StrasbourgFrance June, 1993
   Google Scholar
• Dincol G., Dincol K., Erdem SL., Pobedimskaya D. D., Molchanova T. P., Ye Z., Webber B. B., Wilson J. B., Huisman T. H. J. Hb CLapa or α294(G1)AspGlyβ2, a mildly unstable variant with an AG (GACG`C) mutation in codon 94 of the α1‐globin gene. Hemoglobin 1994; 18: 57
   PubMed Web of Science ®Google Scholar
• Morle F., Francina A., Philippe N., Souillet G., Godet J. Hb Sallanches, a new a chain variant ‘α2 104(G11)CysTyr’ associated with Hb H disease in one homozygous patient. Abstract, Journees Scientifiques du Club de L'Hemoglobine. StrasbourgFrance June, 1993
   Google Scholar
• Wajcman H., Kalmes G., Groff P., Prome D., Riou J., Galacteros F. Hb Melusine ‘α1 14(GH2)ProSer’: A new neutral hemoglobin variant. Hemoglobin 1993; 17: 397
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., M'Rad A., Marden M. C., Riou J., Galacteros F. Hb Val de Marne ‘α133(H16)SerArg’: A new hemoglobin variant with moderate increase in oxygen affinity. Hemoglobin 1993; 17: 407
   PubMed Web of Science ®Google Scholar
• Owen M. C., Hendy J. G. Hb Footscray or α133(H16)SerArg: A new hemoglobin variant. Hemoglobin 1994; 18: 19
   PubMed Web of Science ®Google Scholar
• Langdown J. V., Williamson D., Beresford C. H., Gibb I., Taylor R., Deacon‐Smith R. A new β chain variant, Hb Tyne ‘β5(A2)ProSer’. Hemoglobin 1994; 18: 333
   PubMed Web of Science ®Google Scholar
• Krishnan K., Martinez F., Wille R. T., Jones R. T., Shih D. T., Head C., Fairbanks V. F., Dabich L. Hb Washtenaw ‘β11(A9)ValPhe’: An electrophoretically silent, unstable, low oxygen affinity variant associated with anemia and chronic cyanosis. Hemoglobin 1994; 18: 285
   PubMed Web of Science ®Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Amernick R., Druskin M. S., Webber B. B., Wilson J. B., Huisman T. H. J. Hb Sinai‐Baltimore or α2β218(A15) ValGly, a silent, mildly unstable β chain variant detected by isoelectrofocusing and high performance liquid chromatography. Hemoglobin 1993; 17: 505
   PubMed Web of Science ®Google Scholar
• Coleman M. B., Lu Z. ‐H., Smith C. M., II, Adams J. G., III, Harrell A., Plonczynski M., Steinberg M. H. Two missense mutations in the β‐globin gene can cause severe β thalassemia. Hemoglobin Medicine Lake (β32‘B14’leucmeglutamine; 98‘FG5’valinemethionine. J. Clin. Invest 1995; 95: 503
   PubMed Web of Science ®Google Scholar
• Owen M. C., Ockelford P. A., Wells R. M. G. Hb Howick ‘β37 (C3)TrpGly’: A new high oxygen affinity variant of the α1β1 contact. Hemoglobin 1993; 17: 513
   PubMed Web of Science ®Google Scholar
• Stabler S., Jones R. T., Head C., Shih D. T. B., Fairbanks V. F. Hemoglobin Denver, beta 41 (C7) PheSer: A low O2 affinity Hb variant associated with chronic cyanosis and hemolysis. Blood 1993; 82(Suppl. 1)222a
   Google Scholar
• Molchanova T. P., Postnikov Yu. V., Pobedimskaya D. D., Smetanina N. S., Moschan A. A., Kazanetz E. G., Tokarev Yu. N., Huisman T. H. J. Hb Aleshaor α2β267(E11)ValMet: A new unstable hemoglobin variant identified through sequencing of amplified DNA. Hemoglobin 1993; 17: 217
   PubMed Web of Science ®Google Scholar
• Fay K. C., Brennan S. O., Costello J. M., Potter H. C., Williamson D. A., Trent R. J., Ockelford P. A., Boswell D. R. Haemoglobin Manukau β67(E11)ValGly: Transfusion‐dependent haemolytic anaemia ameliorated by coexisting alpha thalassemia. Br. J. Haematol 1993; 85: 352
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Prome D., Galacteros F., Gilsanz F. Hb Villaverde ‘β89(F5)SerArg’: The structural modification of an intra‐subunit contact is responsible for a high oxygen affinity. Biochim. Biophys. Acta 1994; 1225: 89
   Web of Science ®Google Scholar
• Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T. P., Huisman T. H. J. Hb Hradec Kralove (Hb HK) or α2β2115(G17)Ala Asp, a severely unstable hemoglobin variant resulting in a dominant β‐thalassemia trait in a Czech family. Hemoglobin 1993; 17: 319
   PubMed Web of Science ®Google Scholar
• Girodon E., Ghanem N., Vidaud M., Riou J., Martin J., Galacteros F., Goossens M. Rapid molecular characterization of mutations leading to unstable hemoglobin β‐chain variants. Ann. Hematol 1992; 65: 188
   PubMed Web of Science ®Google Scholar
• North M. L., Duwig I., Kister J., Bergerat J. P., Oberling F., Groell J. J., Lampert E., Lonsdorfer J., Galacteros F. Hb Puttelange ‘β140(H18)AlaVal’: A new high oxygen affinity variant identified by mass/mass spectrometry. Abstract, Journees Scientifiques du Club de L'Hemoglobin. StrasbourgFrance June, 1993
   Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Huisman T. H. J., Harding S. R., Bakanec R. Hb F‐Saskatoon or α2Gγ221(B3)GluLys observed in a North American Indian newborn. Hemoglobin 1993; 17: 547
   PubMed Web of Science ®Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Gu L. ‐H., Molina M. A., de Pablos J. Ma., Huisman T. H. J. Hb F‐Sacromonte or α2Gγ259(E3) LysGln observed in a Spanish new‐born and his mother. Hemoglobin 1993; 17: 269
   PubMed Web of Science ®Google Scholar
• Ferranti P., Barone F., Pucci P., Malorni A., Marino G., Pilo G., Manca L., Masala B. Hb F‐Sassari: A novel Gγ variant with a threonine residue at position γ75, characterized by mass spectrometric techniques. Hemoglobin 1994; 18: 307
   PubMed Web of Science ®Google Scholar
• Qin W. ‐B., Ju T. ‐L., Yue X. ‐L., Yan X. ‐L., Qin L. ‐Y., Molchanova T. P., Pobedimskaya D. D., Huisman T. H. J. Hb A2‐Liangcheng ‘δ117(G19)AsnAsp (AACG´C)’: A new δ chain variant detected by gene analysis in a Chinese family. Hemoglobin 1993; 17: 463
   PubMed Web of Science ®Google Scholar
• Galacteros F., Girodon E., M'Rad A., Martin J., Goossens M., Jaber L., Cohen I. J., Tamary H., Goshen Y., Zaizov R., Wajcman H. Hb Taybe (α38 or 39 THR deleted): an α‐globin defect, silent in the heterozygous state and producing severe hemolytic anemia in the homozygous. C. R. Acad. Sci 1994; 317: 437
   PubMed Web of Science ®Google Scholar
• Fujisawa K., Yamashiro Y., Hattori Y., Ohba Y., Kajita T., Kageyama S., Arita J. Hb Higashitochigi (Hb HT) ‘β24(B6) or β25(B7) glycine deleted’: A new unstable variant expressing cyanosis. Hemoglobin 1993; 17: 467
   PubMed Web of Science ®Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Streichman S., Huisman T. H. J. Compound heterozygosity for two a‐globin gene defects, Hb Taybe (α1; 38 or 39 minus Thr) and a poly A mutation (α2; AATAAA AATAAG), results in a severe hemolytic anemia. Am. J. Hematol 1994; 47: 198
   PubMed Web of Science ®Google Scholar
• Wajcman H., Bost M., Blouquit Y., Préhu C., Riou J., Galacteros F. Two new α chain variants found during glycated hemoglobin screening: Hb Tatras ‘α7(A5)LysAsn’ and Hb Lisbon ‘α23(B4)Glu Asp’. Hemoglobin 1994; 18: 427
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Imai K., Murakami T., Matsubara H. Hb Kurosaki ‘α7(A5)LysGlu’: A new a chain variant found in a Japanese woman. Hemoglobin 1995; 19: 197
   PubMed Web of Science ®Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Huisman T. H. J. Hb Ramona or α224(B5)TyrCysβ2. Hemoglobin 1994; 18: 365
   PubMed Web of Science ®Google Scholar
• Wajcman H., de Montalembert M., Girot R., Kister J., Maier‐Redel sperger M., Galacteros F. The use of staphylococcus V8 protease in the structural determination of human hemoglobin variants: Hb Valparaiso ‘α88(F9)AlaGly’ as example. Hemoglobin 1994; 18: 275
   PubMed Web of Science ®Google Scholar
• Kister J., Kiger L., Francina A., Hanny P., Szymanowicz A., Blouquit Y., Promě D., Galacteros F., Delaunay J., Wajcman H. Hb Roanne ‘α94(G1)AspGlu’: A variant of the α1β2 interface with an unexpected high oxygen affinity. Biochim. Biophys. Acta 1995; 1246: 34
   PubMed Web of Science ®Google Scholar
• Kazanetz E. G., Leonova J. Ye., Wilson J. B., McMillan S. K., Walbrecht M., de Pablos Gallego J. Ma, Huisman T. H. J. Hb Anamosa or α2111(G18)AlaVaip2 (α2 mutation) and Hb Mulhacen or α2123(H6) AlaSerβ2 (al mutation) are two silent, stable variants detected by sequencing of amplified DNA. Hemoglobin 1995; 19: 1
   PubMed Web of Science ®Google Scholar
• Darbellay R., Mach‐Pascual S., Rose K., Graf J., Beris Ph. Haemoglobin Tuniz‐Bizerte: a new α1 globin 129 LeuPro unstable variant with thalassaemic phenotype. Br. J. Haematol 1995; 90: 71
   PubMed Web of Science ®Google Scholar
• Landin B., Berglund S., Lindoff B. Hb Trollhättan ‘β20(B2)ValGlu’ ‐ a new haemoglobin variant with increased oxygen affinity causing erythrocytosis. Eur. J. Haematol 1994; 53: 21
   PubMed Web of Science ®Google Scholar
• Gürgey A., Altay CL., Gu L. ‐H., Leonova J. Ye., Delibalta A., Öner C., Huisman T. H. J. Hb Hakkari or α2β231(B13)LeuArg, a severely unstable hemoglobin variant associated with numerous intraerythroblastic inclusions and erythroid hyperplasia of the bone marrow. Hemoglobin 1996; 19: 165
   Web of Science ®Google Scholar
• Vassilopoulos G., Papassotiriou J., Voskaridou E., Stamoulakatou A., Premetis E., Galacteros F., Wajcman H., Loukopoulos D. Hemoglobin Arta: A new unstable hemoglobin with reduced oxygen affinity in‐trans with β‐thalassemia. Abstract 255. Br. J. Haematol 1994; 87(Suppl. 1)
   Google Scholar
• Rochette J., Barnetson R., Kiger L., Kister J., Littlewood T. J., Webster R., Poyart C., Thein S. L. Association of a novel high oxygen affinity haemoglobin variant with δβ thalassaemia. Br. J. Haematol 1994; 86: 118
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Katuki T. Hb Yaizu ‘β79(EF3)AspAsn’: A new β chain variant found in a Japanese female. Hemoglobin 1995; 19: 21
   PubMed Web of Science ®Google Scholar
• Wajcman H., Behnken L. J., Riou J., Galacteros F. Hb Mainz ‘β98(FG5)ValGlu’: A new unstable variant carrying a structural modification at the same position as Hb Koln. Abstract 258. Br. J. Haematol 1994; 87(Suppl. 1)
   Google Scholar
• Wajcman H., Kister J., M'Rad A., Promé D., Milpied N., Rapp M. J., Harousseau J. L., Riou J., Bardakdjian J., Galacteros F. Hb Saint Nazaire (β103‘G5’PheIle): A new example of polycythemia due to a hemoglobin variant with increased oxygen affinity. Am. J. Hematol 1993; 44: 16
   PubMed Web of Science ®Google Scholar
• Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J. S. Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora ‘β139 (H17)AsnTyr’. Hemoglobin 1995; 19: 335
   PubMed Web of Science ®Google Scholar
• Abbes S., Fitzgerald P. A., Varady E., Girot R., Pic P., Blouquit Y., Ducrocq R., Drupt F., Wajcman H. Two fetal hemoglobin variants affecting the same residue: Hb F‐Emirates ‘Gγ59(E3)LysGlu’ and Hb F‐Foch ‘Gy59(E3)LysGln’. Hemoglobin 1995; 19: 173
   PubMed Web of Science ®Google Scholar
• Plaseska D., Panovska‐Popovska S., Lazervski M., Efremov G. D. Hb F‐Macedonia‐II ‘Gγ104(G6)LysAsn’: A new γ chain variant. Hemoglobin 1994; 18: 373
   PubMed Web of Science ®Google Scholar
• Plaseska D., Cepreganova‐Krstik B., Momirovska A., Efremov G. D. Hb F‐Macedonk‐I or α2Aγ22(NA2)HisGln. Hemoglobin 1994; 18: 241
   PubMed Web of Science ®Google Scholar
• Loudianos G., Porcu S., Cossu P., Tannoia N., Vitucci A., Campanale D., Cao A., Pirastu M. A new δ‐chain variant Hemoglobin A2‐Puglia or α2δ2 26 GluAsp (B8), detected by DNA analysis in a family of Southern Italian origin. Hum. Mut 1993; 2: 327
   PubMed Web of Science ®Google Scholar
• Galanello R., Gasperini D., Perseu L., Barella S., Ideo A., Cao A. Hb A2‐Sant' Antioco ‘α2δ293(F9)CysGly’: A new δ chain variant identified by sequencing of amplified DNA. Hemoglobin 1994; 18: 437
   PubMed Web of Science ®Google Scholar
• Préhu M. ‐O., Préhu C., Goossens M., Galactéros F., Wajcman H. A new anti‐Lepore hemoglobin, Hb β India (β87‐δ105), found in coincidence with a CG substitution at position 162 of IVS‐2 in both the δ and βδ genes, questions on the genetic mechanisms leading to Hbs Lepore and anti‐Lepore. Blood 1994; 83(Suppl. 1)261a
   Google Scholar
• Waye J. S., Eng B., Patterson M., Chui D. H. K., Olivieri N. F. Identification of a novel termination codon mutation (TAAT´T, Term Tyr) in the α2 globin gene in a Laotian girl with Hemoglobin H disease. Blood 1994; 83: 3418
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kister J., Promé D., Blouquit Y., Préhu C., Poyart C., Galactéros F. Interaction of 2 amino acid substitutions within the same β chain of human hemoglobin: the examples of Hb Corbeil and Hb Villeparisis. C. R. Acad. Sci 1995; 318: 785
   PubMed Web of Science ®Google Scholar
• Wajcman H., Blouquit Y., Laharry A., Soummer A. M., Groff P., Bardakdjian J., Préhu C., Riou J., Godard C., Galactèros F. Three new neutral a chain variants: Hb Bois Guillaume ‘α65(E14)AlaVal’, Hb Mantes‐La‐Jolie ‘α79(EF8)AlaThr’, and Hb Mosella ‘α111(G18) AlaThr’. Hemoglobin 1995; 19: 281
   PubMed Web of Science ®Google Scholar
• Giordano P. C., Harteveld C. L., Kok P. J. M. J., Geenen A., Batelaan D., Amons R., Bernini L. F. Hb Gouda‘α72(EF1)HisGln’, anew silent α chain variant. Hemoglobin 1996; 20: 21
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Uehara S., Matsushita K. Two new a chain variants: Hb Fuchu‐I ‘α72(EF1)HisTyr’ and Hb Fuchu‐II ‘α97 (G4)AsnHis’. Hemoglobin 1995; 19: 389
   PubMed Web of Science ®Google Scholar
• Wajeman H., Promé D., Riou J., Mathis M., Godart C., Hurtrel D., Préhu C., Bardakkjian J., Bridey F., Galactéros F. Hb Saclay ‘α133(H16)SerAsn’: a new neutral variant. Abstract 48. Nouv. Rev. Fr. d'Hematol 1996; 38: 27
   Google Scholar
• Harano K., Harano T., Koide G., Akimaru S. Hb Nakano ‘β8 (LysMet’: a new β chain variant found in a Japanese woman. Hemoglobin 1995; 19: 397
   PubMed Web of Science ®Google Scholar
• Beris Ph., Darbellay R., Frutiger A., Hochstrasser D. Hb Iraq‐Halabja 10(a7) AlaVal (THE INDIA LIMITED COMPANYCCGTC): a new β‐chain variant that produces no significant clinical or hematological alterations. Blood 1995; 86(Suppl. 1)642a
   Google Scholar
• Wajeman H., Promé D., Kister J., Davies S. C., Galactéros F., Henthorn J. S. Hb Uxbridge ‘β20(B2)ValGly’: a new hemoglobin variant with mild increase in oxygen affinity found on neonatal screening. Hemoglobin
   Google Scholar
• Lacan P., Francina A., Promé D., Galactéros F., Wajeman H. Hb Aubenas ‘β26(B8)GluGly’: a new variant normally synthesized affecting the same codon as in Hb E. Hemoglobin
   Google Scholar
• Seelig H. P. Hb Karlsruhe ‘β28(B10)LeuMet’: a new unstable β‐globin mutant causing cyanosis and methemoglobinemia. 1995, Personal communication
   Google Scholar
• Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M. C., Cao A., Breitenstein U., Fehr J., Tuchschmid P. Hb Hinwil or β38(C4)ThrAsn: a new β chain variant detected in a Swiss family. Hemoglobin
   Google Scholar
• Kiger L., Groff P., Kalmes G., Kister J., Promé D., Galactéros F., Wajeman H. Hb J‐Europa‘β62(E6)AlaAsp’: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin
   Google Scholar
• Rodriguez Romero W. E., Castillo M., Chaves M. A., Saenz G. F., Gu L. ‐H., Wilson J. B., Baysal E., Smetanina N. S., Leonova J. Y., Huisman T. H. J. Hb Costa Rica or α2β277(EF1)HisArg: the first example of a somatic cell mutation in a globin gene. Hum. Genet
   Google Scholar
• Ohba Y., Yamada H., Takamatsu S., Imai K. Hb Tsurumai ‘β82 (EF6)LysGln’: a new Hb variant with high oxygen affinity and erythrocytosis. Hemoglobin
   Google Scholar
• Lacan P., Kister J., Francina A., Souillet G., Galactéros F., Delaunay J., Wajeman H. Hemoglobin Debrousse(β96‘FG3’LeuPro): anew unstable hemoglobin with twofold increased oxygen affinity. Am. J. Hematol 1996; 51: 276
   PubMed Web of Science ®Google Scholar
• Kister J., Papassotiriou I., Groff P., Kalmes G., Promé D., Wajcman H. Structural and functional characterisation of a new electrophoretically silent hemoglobin variant. Abstract 46. Nouv. Rev. Fr. d'Hematol 1996; 38: 26
   Google Scholar
• Gray G. R., Manson H. E., Gu L. ‐H., Leonova J. Ye., Huisman T. H. J. Hb Lulu Island(α2β2107‘G9’GlyAsp)‐βd`‐thalassemia(codon 15; TTHE INDIA LIMITED COMPANYGT´G), a form of thalassemia intermedia. Am. J. Hematol 1995; 50: 26
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Kawasaki R., Kawakami K. Hb Toranomon ‘β112(G14)CysTrp’: a new unstable and electrophoretically silent hemoglobin variant. Hemoglobin
   Google Scholar
• Hutt P. J., Griffin T., Fairbanks V., Hoyer J., Thibodeau S. Hemoglobin Cook, β132(H10) LysThr, a new unstable Hb variant encountered in a SE Asian. Blood 1995; 86(Suppl. 1)649a
   Google Scholar
• Fairbanks V., McCormick D., Horn A., Jones R., Shih D., Hoyer J., Madden B. J., Kubik K. Hemoglobin Old Dominion, β143 (H21) HisTyr: a new variant causing spurious elevation of Hb Ale. Blood 1995; 86(Suppl. 1)647a
   Google Scholar
• de Pablos Gallego J. Ma, Gu L. ‐H., Leonova J. Ye., Huisman T. H. J. Hb F‐Veleta or α2Gγ240(C6)ArgGly. Hemoglobin 1995; 19: 407
   PubMed Web of Science ®Google Scholar
• Kohli‐Kumar M., Zwerdling T., Rucknagel D. L. Hemoglobin F‐Cincinnati, α2Gγ241(C7) PheSer in a Newborn with cyanosis. Am. J. Hematol 1995; 49: 43
   PubMed Web of Science ®Google Scholar
• Wajcman H., Ducrocq R., Promé D., Galactéros F. Hb F‐Mauritius ‘Aγ 23 (B5) Ala deleted’: evidence for an identical hotspot for deletions in the various β‐like genes. C. R. Acad. Sci 1995; 318: 1065
   PubMed Web of Science ®Google Scholar
• Gu L. ‐H., Oner C., Huisman H. The GγT chain (Gγ75; 136 Gly) in Hb F‐Charlotte is the product of an Aγ gene with a limited gene conversion and that in Hb F‐Waynesboro of a mutated Gy gene. Hemoglobin 1995; 19: 413
   PubMed Web of Science ®Google Scholar
• Papadakis M., Drakoulakou O., Papapanagiotou E., Pessini D., Loutradi‐Anagnostou A. Hb A2‐Agrinio ‘δ43(CD2)GluGly (THE INDIA LIMITED COMPANYAG THE INDIA LIMITED COMPANYTHE INDIA LIMITED COMPANYG)’: A new δ chain variant detected in a Greek family. Hemoglobin 1995; 19: 295
   PubMed Web of Science ®Google Scholar
• Kaeda J., Jarvis M., Kokal I., Reeves J., Vulliamy T., Luzzatto L. A new double mutant Hb C‐Rothschild. Abstract Book. 5th International Conference on the Thalassaemias and the Haemoglobinopathies. Nicosia, Cyprus 1993; 215
   Google Scholar