International Hemoglobin Information Center: Policies—Ihic

References

• Crookston J. H., Beale D., Irvine D., Lehmann H. A new Haemoglobin J Toronto (α5 Alanine→Aspartic acid). Nature 1965; 208: 1059–1061
   PubMed Web of Science ®Google Scholar
• Sumida I., Ohta Y., Imamura T., Yanase T. Hemoglobin Sawara: α6(A4) Aspartic acid6αanine. Biochim. Biophys. Acta 1973; 322: 23–26
   PubMed Web of Science ®Google Scholar
• Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M. Increased oxygen affinity for Hemoglobin Sawara: aLA4(6) Aspartic acidαanine. Biochim. Biophys. Acta 1977; 495: 183–186
   PubMed Web of Science ®Google Scholar
• Jue D. L., Johnson M. H., Patchen L. C., Hoo‐Penn W. F. Hemoglobin Dunn: α6(A4) Aspartic acid→Asparagine. Hemoglobin 1979; 3: 137–143
   PubMed Web of Science ®Google Scholar
• Pootrakul S., Kematorn B., Na‐Nakorn S., Suanpan S. A new haemoglobin variant: Haemoglobin Anantharaj alpha 11 (A9) Lysine→Glutamic acid. Biochim. Biophys. Acta 1975; 405: 161–166
   PubMed Web of Science ®Google Scholar
• Rosa J., Maleknia N., Vergoz D., Dunet R. Une nouvelle hemoglobine anormale: l'hémoglobin J α Paris 12 Ala→Asp. Nouv. Rev. Fr. D'Hémat. 1965; 6: 423–426
   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: 291–298
   PubMed Web of Science ®Google Scholar
• Marti H. R., Pik C., Mosimann P. Eine neue hämoglobin I variante: Hb I Interlaken. Acta Haematol. 1964; 32: 9–16
   PubMed Web of Science ®Google Scholar
• Liddell J., Brown D., Beale D., Lehmann H., Huntsman R. G. A new haemoglobin ‐ Jα Oxford found during a survey of an English population. Nature 1964; 204: 269–270
   PubMed Web of Science ®Google Scholar
• Silvestroni E., Bianco I., Tentori L., Vivaldi G., Carta S., Sorcini M., Brancati C. (1967) Proc. 10th Congr. Eur. Soc. Hematol., Strasbourg, 1965. Karger, Basel/New York, 232–237, Part II
   Google Scholar
• Vella F., Casey R., Lehmann H., Labossiere A., Jones T. G. Haemoglobin Ottawa: α2 15(A13) Gly→Arg β2. Biochim. Biophys. Acta 1974; 336: 25–29
   Web of Science ®Google Scholar
• Pootrakul S., Srichiyanont S., Wasi P., Suanpan S. Hemoglobin Siam (α2 15 Arg β2): A new a chain variant. Humangenetik 1974; 23: 199–204
   PubMedGoogle Scholar
• Beale D., Lehmann H. Abnormal haemoglobins and the genetic code. Nature 1965; 207: 259–261
   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: 940–946
   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: 816–822
   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: 368–372
   PubMedGoogle Scholar
• Griffiths K. D., Lang A., Lehmann H., Mann J. R., Plowman D., Raine D. N. Haemoglobin Handsworth α18(A16) Glycine→Arginine. FEBS Lett. 1977; 75: 93–95
   PubMed Web of Science ®Google Scholar
• Rahbar S., Ala F., Akhavan E., Nowzari G., Shoa'i I., Zamanianpoor M. H. Two new haemoglobins: Haemoglobin Perspolis [α64 (E13) Asp→Tyr] and Haemoglobin J-Kurosb [α19 (AB1) Ala→Asp]. Biochim. Biophys. Acta 1976; 427: 119–125
   PubMed Web of Science ®Google Scholar
• Kendall A. G., Barr R. D., Lang A., Lehmann H. Haemoglobin J Nyanza: α21 (β2) Ala→Asp. Biochim. Biophys. Acta 1973; 310: 357–359
   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: 886–887
   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 23Glu→Lys β2. Am. J. Hum. Genet. 1968; 20: 570–578
   PubMed Web of Science ®Google Scholar
• Marengo‐Rowe A. J., Beale D., Lehmann H. New human haemoglobin variant from southern Arabia: G‐Audhali (α23 (B4) Glutamic acid→Valine) and the variability of B4 in human haemoglobin. Nature 1968; 219: 1164–1166
   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 Glu→Gly (B8) a variant present in unusually low concentration. Biochim. Biophys. Acta 1971; 243: 164–169
   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 β27 Glu→Val (B8). Biochim. Biophys. Acta 1976; 427: 530–538
   PubMed Web of Science ®Google Scholar
• Vettore L., DeSandre G., Dilorio E. E., Winterhalter K. H., Lang A., Lehmam H. A new abnormal hemoglobin O Padova, α30 (B11) Gla→Lys and a dyserythropoietic anemia with erythroblastic multinuclearity co‐existing in the same patient. Blood 1974; 44: 869–877
   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: 454–455
   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: 460–461
   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: 1517–1520
   Web of Science ®Google Scholar
• Marinucci M., Mavilio F., Tentori L., D'Erasmo F., Cola‐pietro A., De Stasio G., Di Fonzo S. A new human hemoglobin variant: Hb Bari (α2 45(CD3) His→Gln β2). Biochim. Biophys. Acta 1980; 622: 315–319
   PubMed Web of Science ®Google Scholar
• Beretta A., Prato V., Gallo E., Lehmann H. Haemoglobin Torino ‐ α43 (CD1) Phenylalanines‐Valine. Nature 1968; 217: 1016–1018
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Yokoyama M., Numakura H., Nagata K., Takebe Y., Izumi Y., Shibata S. Hemoglobin Hirosaki (α43 [CE 1] Phe→Leu), a new unstable variant. Biochim. Biophys. Acta 1975; 405: 155–160
   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) His→Arg β2) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1977; 493: 228–233
   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 (α2 6A1a β2) and Hemoglobin Mugino (Hb L Ferrara; α2 47Gly β2). Jap. J. Hun. Genet. 1975; 19: 343–363
   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: 484–486
   PubMed Web of Science ®Google Scholar
• Halbrecht I., Isaacs W. A., Lehmann H., Ben‐Porat F. Hemoglobin Hasharon (α47 Aspartic acid→Histidine). Israel J. Med. Sci. 1967; 3: 827–831
   PubMedGoogle Scholar
• Ostertag W., Smith E. W. Hb Sinai: A new α chain mutant α47 His. Humangenetik 1968; 6: 377–379
   PubMedGoogle Scholar
• Schneider R. G., Ueda S., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sealy (α2 47 His β2): A new variant in a Jewish family. Am. J. Hum. Genet. 1968; 20: 151–156
   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: 395–396
   PubMed Web of Science ®Google Scholar
• Tentori L. Hemoglobin L Ferrara ϵ Hemoglobin Hasharon. Hemoglobin 1977; 1: 602
   Google Scholar
• Rahbar S., Mahdavi N., Nowzari G., Mostafavi I. Hemoglobin Arya: α2 47(CD5) Aspartic acid→Asparagine. Biochim. Biophys. Acta 1975; 386: 525–529
   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 (α39 (C5) Gln→Lys) and Hemoglobin Montgomery (α46 (CD6) teu→Arg). Biochim. Biophys. Acta 1975; 379: 28–32
   PubMed Web of Science ®Google Scholar
• Tangheroni W., Zorcolo G., Gallo E., Lehmann H. Haemoglobin J Sardegna: α50 (CD8) Histidine→Aspartic acid. Nature 1968; 218: 470–471
   PubMed Web of Science ®Google Scholar
• Cabarmes R., Renaud R., Mauran A., Pennors H., Charlesworth D., Price B. G., Lehmann H. Deux hémoglobines rapides an Cote‐D'Ivoire: 1'Hb K Woolwich et une nouvelle hémoglobine, 1'Hb J Abidjan (α51 Gly→Asp). Nouv. Rev. Fr. D'Hémat. 1972; 12: 289–300
   PubMedGoogle Scholar
• Reynolds C. A., Huisman T. H. J. Hemoglobin Russ or α2 51 Arg β2. Biochim. Biophys. Acta 1966; 130: 541–543
   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) Alanine→Aspartic acid. Biochim. Biophys. Acta 1974; 342: 1–4
   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: 531–536
   PubMedGoogle Scholar
• Jones R. T., Brimhall B., Lisker R. Chemical characterization of Hemoglobin Mexico and Hemoglobin Chiapas. Biochim. Biophys. Acta 1968; 154: 488–495
   PubMed Web of Science ®Google Scholar
• Rosa J., Labie D., Maleknia N., Blum N. Sur quelques hémoglobines anormales nouvelles recemtnent isolées en France. International Symposium on Comparative Hemoglobin Structure, Thessaloniki, April, 11–131966, 140–145
   Google Scholar
• Fessas Ph., Kaltsoya A., Loukopoulos D., Nilsson L. ‐O. On the chemical structure of Haemoglobin Uppsala. Hum. Hered. 1969; 19: 152–158
   PubMed Web of Science ®Google Scholar
• Pootrakul S., Boonyarat D., Kematorn B., Suanpan S., Wasi P. Hemoglobin Thailand [α56 (E5) Lys→Thr]: A new abnormal human hemoglobin. Hemoglobin 1977; 1: 781–798
   PubMed Web of Science ®Google Scholar
• Rahbar S., Kinderlerer J. L., Lehmann H. Haemoglobin L Persian Gulf: α57 (E6) Glycine→Arginine. Acta Haematol. 1969; 42: 169–175
   PubMed Web of Science ®Google Scholar
• Baglioni C. A chemical study of Hemoglobin Norfolk. J. Biol. Chem. 1962; 237: 69–74
   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: 584–593
   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: 40–53
   Google Scholar
• Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb H. Proc. Natl. Acad. Sci. USA 1961; 47: 1758–1767
   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: 472–482
   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: 503–511
   PubMedGoogle Scholar
• Hollán S. R., Szelétiyi J. G., Lehmann H., Beale D. A Boston‐type Haemoglobin M in Hungary: Haemoglobin M Kiskunhalas. Haematologia 1967; 1: 11–18
   Google Scholar
• Barclay G. P. T., Charlesworth D., Lehraarm H. Abnormal haemoglobin in Zambia. A new Haemoglobin Zambia α60 (E9) Lysine→Asparagine. Br. Med. J. 1969; 4: 595–596
   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) Lys→Asn) and G Pest (α74 (EF3) Asp→Asn). Biochim. Biophys. Acta 1974; 336: 344–360
   Web of Science ®Google Scholar
• Thillet J., Blouquit Y., Perrone E., Rosa J. Hemoglobin Pontoise α63Ala→Asp (E12). A new fast mowing variant. Biochim. Biophys. Acta 1977; 491: 16–22
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T. S., Tan T. G. H., Weng M. ‐I., Liu C. ‐S., Wang C. ‐L. Hemoglobin G Waimanalo: α64 Asp→Asn. Biochim. Biophys. Acta 1973; 322: 27–33
   PubMed Web of Science ®Google Scholar
• Ramot B., Kinderlerer J. B., Lehmann H. Cited in WHO Technical Report Series No. 509, Geneva 1972, Annex 1
   Google Scholar
• Sukumaran P. K., Merchant S. M., Desai M. P., Wiltshire B. G., Lehmann H. Haemoglobin Q India (α64(E13) Aspartic acid→Histidine) associated with β‐thalassemia observed in three Sindhi families. J. Med. Genet. 1972; 9: 436–442
   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: 347–352
   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: 47–60
   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: 1305–1306
   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: 137–167
   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: 144–148
   PubMed Web of Science ®Google Scholar
• Colombo B., Vidal H., Kamuzora H., Lehmann H. A new Haemoglobin J‐Habana α71 (E20) Alanine→Glutamic acid. Biochim. Biophys. Acta 1974; 351: 1–6
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Daneshmand P. Hemoglobin Daneskgah‐Tehran α2 72 (EF1) Histidine→Arginine β2A. Nature New Biol. 1973; 245: 268–269
   PubMedGoogle Scholar
• Pootrakul S., Dixon G. H. Hemoglobin Mahidol: A new hemoglobin α‐chain mutant. Can. J. Biochem. 1970; 48: 1066–1078
   PubMedGoogle Scholar
• Blackwell R. Q., Liu C. ‐S. Hemoglobin G Taichung: α74 Asp→His. Biochim. Biophys. Acta 1970; 200: 70–75
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Charlesworth D., Lehmann H., Rahbar S., Tuchinda S., Lie‐Injo L. E. Two Haemoglobins Q, α74 (EF3) and α75 (EF4) Aspartic acid→Histidine. Br. J. Haematol. 1970; 19: 117–125
   PubMed Web of Science ®Google Scholar
• Orringer E. P., Wilson J. B., Huisman T. H. J. Hemoglobin Chapel Hill or α2 74 Asp→Gly β2. FEBS Lett. 1976; 65: 297–300
   PubMed Web of Science ®Google Scholar
• Vella F., Wiltshire B., Lehmann H., Galbraith P. Hemoglobin Winnipeg α2 75 Asp→Tyr β2. Clin. Biochem. 1973; 6: 66–70
   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 acid→Asparagin. Hemoglobin 1977; 1: 383–388
   PubMed Web of Science ®Google Scholar
• Van Ros G., Beale O., Lehmann H. Haemoglobin Stanley‐ville‐II (α78 Asparagine→Lysine). Br. Med. J. 1968; 4: 92–93
   PubMed Web of Science ®Google Scholar
• Rucknagel D. L., Brandt N. J., Spencer H. H. aα‐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: 1427–1429
   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 Ser→Cys), a new variant having an inhibitory effect on the gelation of 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 α82 Ala→Asp. 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: 143–146
   PubMedGoogle Scholar
• Huehns E. R. The unstable hemoglobins. Bull. Soc. Chem. Biol. 1970; 52: 1131–1146
   PubMedGoogle Scholar
• Lorkin P. A., Huntsman R. G., Ager J. A. M., Lehmann H., Vella F., Darbre P. D. Haemoglobin G Norfolk: α85 (F6) Asp→Asn. Biochim. Biophys. Acta 1975; 379: 22–27
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Manasse B., Thillet J., Rosa J. Haemoglobin G Norfolk α85 (F6) Asp→. Structural characterization by sequenator analysis and functional properties of a new variant with high oxygen affinity. FEBS Lett. 1975; 50: 163–167
   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: 35–39
   PubMedGoogle Scholar
• Reed R. E., Winter W. P., Rucknagel D. L. Haemoglobin Inkster (α2 85 Aspartic acid→Valine β2) coexisting with β‐thalassemia in a Caucasian family. Br. J. Haematol. 1974; 26: 475–484
   PubMed Web of Science ®Google Scholar
• Knuth A., Pribilla W., Marti H. R., Winterhalter K. H. Hemoglobin Moabit: Alpha 86 (F7) Leu→Arg. A new unstable abnormal hemoglobin. Acta Haematol. 1979; 61: 121–124
   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: 538–543
   PubMedGoogle Scholar
• Heller P., Weinstein H. G., Yakulis V. J., Rosenthal I. M. Hemoglobin M Kankakee, a new variant of Hemoglobin H. Blood 1962; 20: 287–301
   PubMed Web of Science ®Google Scholar
• Pik C., Tönz 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 décrite, dans une famille Francaise. Compt. R. Sceanc. Soc. Biol. 1966; 160: 2270–2272
   PubMed Web of Science ®Google Scholar
• Vella F., Charlesworth D., Lorkin P. A., Lehmann H. Hemoglobin Broussais α90 Lys→Asn. Can. J. Biochem. 1970; 48: 908–910
   PubMedGoogle Scholar
• Braconnier F., Cohen‐Solal H., Schlegel N., Blouquit Y., Thillet J., Cassius De Linval J., Rosa J. Hemoglobin J. Broussais α2 90 Lys→Asn β2A (FG2), decouverte dans une famille Martiniquaise. Nouv. Rev. Fr. D'Hemat. 1975; 15: 333–342
   PubMedGoogle Scholar
• Hyde R. O., Kinderlerer J. L., Lehmann H., Hall M. D. Haemoglobin 3 Rajappen: α90 (FG2) Lys→Thr. Biochira. Biophys. Acta 1971; 247: 515–519
   Google Scholar
• Brennan S. O., Tauro G. P., Melrose W., Carrell R. W. Haemoglobin Port Phillip α91 (FG3) Leu→Pro. A new unstable haemoglobin. FEBS Lett. 1977; 81: 115–117
   PubMed Web of Science ®Google Scholar
• Botha M. C., Beale D., Isaacs W. A., Lehmann H. Haemo‐globin J Cape Town α2 92 Arginine→Glutamine β2. Nature 1966; 212: 792–795
   PubMed Web of Science ®Google Scholar
• Lines J. G., McIntosh R. Oxygen binding by Haemoglobin J Cape Town (α2 92 Arg→Gln). Nature 1967; 215: 297–298
   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. Hoi. Biol. 1966; 19: 91–108
   Google Scholar
• Charache S., Weatherall D. J., Clegg J. B. Polycythemia associated with a hemoglobinopathy. J. Clin. Invest. 1966; 45: 813–822
   PubMed Web of Science ®Google Scholar
• Wajcman H., Belkhodja O., Labie D. Hb Setif: G1(94) αAsp→Tyr. A new α chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits. FEBS Lett. 1972; 27: 298–300
   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 Asp→Asp, a new haemoglobin with a lowered affinity for oxygen. Biochim. Biophys. Acta 1975; 400: 365–373
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Shelton J. B., Shelton J. R., Powars D. Hemoglobin Sunshine Seth ‐ α2 (94CG1) Asp→His) β2. Hemoglobin 1979; 3: 145–159
   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 α2 95 Leu (G2) β2. Biochim. Biophys. Acta 1970; 200: 578–580
   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: 1433–1439
   PubMed Web of Science ®Google Scholar
• De Jong W. W. W., Bernini L. F., Meera Khan P. Haemoglobin Rampa: α95 Pro→Ser. Biochim. Biophys. Acta 1971; 236: 197–200
   PubMed Web of Science ®Google Scholar
• Wiltshire B. G., Clark K. G. A., Lorkin P. A., Lehmann H. Haemoglobin Denmark Hill α95 (G2) Proαa, a variant with unusual electrophoretic and oxygen binding properties. Biochim. Biophys. Acta 1972; 278: 459–464
   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: 301–307
   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: 911–914
   PubMedGoogle Scholar
• Sanguansermsri T., Matragoon S., Changloah L., Flatz G. Hemoglobin Suan‐Dok (α2 109 (G16) Leu→Arg β2): An unstable variant associated with α‐thalassemia. Hemoglobin 1979; 3: 161–174
   PubMed Web of Science ®Google Scholar
• Charache S., Ostertag W. Hemoglobin Hopkins‐2 ((α112 Asp) 2 β2): “Low output” protects from potentially harmful effects. Blood 1970; 36: 852
   Google Scholar
• Clegg J. B., Charache S. The structure of Hemoglobin Hopkins‐2. Hemoglobin 1978; 2: 85–88
   PubMed Web of Science ®Google Scholar
• Niazi G. A., Efremov G. D., Nikolov N., Hunter E., Jr., Huisman T. H. J. Hemoglobin Strumica or α2 112(G19) His→Arg β2. (With an addendum: Hemoglobin J Paris‐I α2 12 A10) Ala→Asp β2 in the same population.). Biochim. Biophys. Acta 1975; 412: 181–186
   PubMed Web of Science ®Google Scholar
• Beksedic D., Rajevska T., Lorkin P. A., Lehmann H. Hb Serbia (α112(G19) His→Arg), a new haemoglobin variant from Yugoslavia. FEBS Lett. 1975; 58: 226–229
   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 Alanine→Aspartic acid): The first new haemoglobin variant found in a Pacific (Melanesian) population. J. Med. Genet. 1967; 4: 1–6
   PubMedGoogle Scholar
• Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229–232
   PubMed Web of Science ®Google Scholar
• Lie‐Injo L. E., Sadono. Haemoglobin O (Buginese X) in Sulawesi. Br. Med. J. 1958; 1: 1461–1462
   PubMed Web of Science ®Google Scholar
• Sansone G., Centa A., Sciarratta V., Gallo E., Lehmann H. Haemoglobin O Indonesia (α116 Glu→Lys) in an Italian family. Acta Haematol. 1970; 43: 40–47
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Morito M., Iuchi I. Characterization of Hb Ube‐4: Alpha 116 (GH4) Gluαa. Hemoglobin 1978; 2: 181–186
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Wong Hock Boon, Wang C. ‐L., Weng M. ‐I., Liu C. ‐S. Hemoglobin J Meerut: α120 Ala→Glu. Biochim. Biophys. Acta 1974; 351: 7–12
   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) Ala→Glu. Ann. Clin. Biochem. 1974; 11: 53–55
   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) Asp→Asn. A new hemoglobin variant in the α1β1 contact region showing high oxygen affinity and reduced cooperativity. Biochim. Biophys. Acta 1977; 490: 443–451
   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) Lys→Thr β2. Biochim. Biophys. Acta 1974; 365: 318–322
   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. H. Hemoglobin Jackson, α127 (H10) Lys→Asn. Am. J. Clin. Pathol. 1976; 66: 453–456
   PubMed Web of Science ®Google Scholar
• Kleihauer E. F., Reynolds C. A., Dozy A. M., Wilson J. B., Hoores R. R., Berertson M. P., Wright C. ‐S., Huisman T. H. J. Hemoglobin Bibba or α2 136 Pro β2, an unstable α‐chain abnormal hemoglobin. Biochim. Biophys. Acta 1968; 154: 220–222
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Wong Hock Boon, Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 222: 379–380
   PubMed Web of Science ®Google Scholar
• Poyart C., Krishnamoorthy R., Bursaux E., Gacon G., Labie D. Structural and functional studies of Haemoglobin Suresnes or α2141 (HC3) Arg→His β2, a new high oxygen affinity mutant. FEBS Lett. 1976; 69: 103–107
   PubMed Web of Science ®Google Scholar
• Saenz G. F., Elizondo J., Alvarado M. A., Atmetlla F., Arroys G., Martinez G., Lima F., Colombo B. Chemical characterization of a new haemoglobin variant Haemoglobin J Cubujuqui (α2 141 (HC3) Arg→Ser β2). Biochim. Biophys. Acta 1977; 494: 48–50
   PubMed Web of Science ®Google Scholar
• Mavilio F., Marinucci M., Tentori L., Fontanarosa P. P., Rossi U., Biagiotti S. Hemoglobin Legnano (α2141 (HC3) Arg→Leu β2): A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1978; 2: 249–259
   PubMed Web of Science ®Google Scholar
• Martinez G., Lima F., Residenti C., Colombo B. Hb J Camagüey α2 141 (HC3) Arg→Gly β2. A new abnormal human hemoglobin. Hemoglobin 1978; 2: 47–52
   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 (β1 Valine→Acetylalanine). Structural and functional characterization. Biochemistry 1977; 16: 4872–4879
   PubMed Web of Science ®Google Scholar
• Labossiere A., Vella F., Hiebert J., Galbraith P. Hemoglobin Deer Lodge: α2β2 His→Arg. Clin. Biochem. 1972; 5: 46–50
   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: 402–411
   PubMed Web of Science ®Google Scholar
• Hunt J. A., Ingram V. M. Abnormal human haemoglobins. IV. The chemical difference between normal human haemo‐globin and Haemoglobin C. Biochim. Biophys. Acta 1960; 42: 409–421
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Oemijati S., Pribadi W., Weng M. ‐I., Liu C. ‐S. Hemoglobin G Makassar: β6 Gluαa. Biochim. Biophys. Acta 1970; 214: 396–401
   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: 3182–3187
   PubMed Web of Science ®Google Scholar
• Tuchinda S., Beale D., Lehmann H. A new haemoglobin in a Thai family. A case of Haemoglobin Siriraj‐8‐thalassaemia. Br. Med. J. 1965; 1: 1583–1585
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Riggs A. Polymerization of hemoglobins of mouse and man. Structural basis. Science 1967; 158: 800–802
   PubMed Web of Science ®Google Scholar
• Tondo C. V., Bonaventura J., Bonaventura C., Brunori M., Antonini E. Functional properties of Hemoglobin Porto Alegre (αA2β92Ser→Cys) and the reactivity of its extra cysteinyl residue. Biochim. Biophys. Acta 1974; 342: 15–20
   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) Ala→Asp). FEBS Lett. 1974; 42: 121–123
   PubMed Web of Science ®Google Scholar
• Monn E., Gaffney P. J., Lehmann H. Haemoglobin Sogn (β14 Argjnine). A new haemoglobin variant. Scand. J. Haematol. 1968; 5: 353–360
   PubMedGoogle Scholar
• Beuzard Y., Basset P., Braconnier F., El Gammel H., Martin L., Oudard J. L., Thillet J. Haemoglobin Saki α2β2 14 Leu→Pro (All) structure and function. Biochim. Biophys. Acta 1975; 393: 182–187
   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) Leu→Pro). Am. J. Hematol. 1976; 1: 283–292
   PubMed Web of Science ®Google Scholar
• Kennedy C. C., Blundell G., Lorkin P. A., Lang A., Lehmann H. Haemoglobin Belfast 15(A12) Tryptopharr→Arginine: A new unstable haemoglobin variant. Br. Med. J. 1974; 4: 324–326
   PubMed Web of Science ®Google Scholar
• Gacon G., Wajcman H., Labie D., Uaret B., Christoforov B. A second case of Haemoglobin Belfast (β15[A12]Trp→Arg) observed in a French patient. Acta Haematol. 1976; 55: 313–319
   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: 637–643
   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: 1–12
   PubMedGoogle Scholar
• Chernoff A. I., Perillie P. E. The amino acid composition of HGB New Haven #2 (HGB N New Haven). Biochim. Biophys. Res. Commun. 1964; 16: 368–372
   PubMed Web of Science ®Google Scholar
• Wong S. C., Bouver N., Wilson J. B., Huisman T. H. J. Hb J Georgia = Hb J Baltimore = α2β216Gly→Asp. Clin. Chim. Acta 1971; 35: 521–522
   PubMed Web of Science ®Google Scholar
• Wade P. T., Jenkins T., Huehns E. R. Haemoglobin variant in a Bushman: Haemoglobin D α Bushman a β22 16Gly→Arg. Nature 1967; 216: 688–690
   PubMed Web of Science ®Google Scholar
• Maekawa M., Maekawa T., Fujiwara N., Tabara K., Matsuda G. Hemoglobin Nagasaki: α2β2(32 17 Glu. A new abnormal human hemoglobin found in one family in Nagasaki. Int. J. Prot. Res. 1970; II: 147–156
   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) Asn→Lys and Hemoglobin D Iran β22(B4) Glu→Gln. Biochim. Biophys. Acta 1973; 310: 360–364
   PubMed Web of Science ®Google Scholar
• Lam H., Wilson J. B., Harris H., Gravely M., Huisman T. H. J. Hemoglobin Alamo [α2β2 19 (β1) Asn→Asp]. Hemoglobin 1977; 1: 703–706
   PubMed Web of Science ®Google Scholar
• Stamatoyannopoulos G., Nute P. E., Adamson J. W., Bellingham A. J., Funk D., Hornung S. Hemoglobin Olympia (β20 Valine→Methionine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J. Clin. Invest. 1973; 52: 342–349
   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 Glu→Lys. Can. J. Biochem. 1967; 45: 1385–1391
   PubMedGoogle Scholar
• Blaekwell R. Q., Yang H. J., Wang C. C. Hemoglobin G Taipei: α2β2 22 Glu→Gly. Biochim. Biophys. Acta 1969; 175: 237–241
   PubMedGoogle Scholar
• Vella F., Isaacs W. A., Lehmann H. Hemoglobin G Saskatoon: β22 Glu→Ala. Can. J. Biochem. 1967; 45: 351–353
   PubMedGoogle Scholar
• Blaekwell R. Q., Liu C. S., Yang H. J., Wang C. C., Huang J. T. H. Hemoglobin variant common to Chinese and North American Indians: α2β2 22 Glu→Ala. Science 1968; 161: 381–382
   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: 466–470
   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 Glu→Ala. Am. J. Phys. Anthropol. 1969; 30: 389–392
   PubMedGoogle Scholar
• Rahbar S. Haemoglobin D Iran: β22 Glutamic acid→Glutamine (B4). Br. J. Haematol. 1973; 24: 31–35
   PubMed Web of Science ®Google Scholar
• Garel H. C., Blouguit Y., Arous N., Rosa J. Hb Strasbourg α2β2 20(B2) Val→Asp: A variant at the same locus as Hb Olympia β20Val→Met. FEBS Lett. 1976; 72: 1–4
   PubMed Web of Science ®Google Scholar
• Forget B. G. Nucleotide sequence of human β globin messenger RNA. Hemoglobin 1977; 1: 879–881
   PubMed Web of Science ®Google Scholar
• Ranney H. H., 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: 1004–1011
   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‐Glycine→Valine): An unstable variant causing anemia with inclusion bodies. J. Clin. Invest. 1971; 50: 650–659
   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) Gly→Asp) found in the U. S. S. R. Nature 1974; 249: 768–770
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S. Hemoglobin G Taiwan‐Ami α2β2 25 Gly→Arg. Biochem. Biophys. Res. Commun. 1968; 30: 690–696
   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: 520–536
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Arous N., Hachado P. E. A., Garel M. C. Hb Henri Mondor: β26 (B8) Glu→Val: A variant with a substitution localized at the same position as that of Hb E β26 Glu→Lys. FEBS Lett. 1976; 72: 5–7
   PubMed Web of Science ®Google Scholar
• Idelson L. I., Didkovsky N. A., Filippova A. V., Casey R., Kynoch P. A. M., Lehmann H. Haemoglobin Volga, β27 (B9) Ala→Asp, a new highly unstable haemoglobin with a suppressed charge. FEBS Lett. 1975; 58: 122–125
   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) Ala→Asp: An unstable hemoglobin variant in three generations of a Dutch family. Biochim. Biophys. Acta 1976; 439: 63–69
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Seligmann M., Thillet J., Rosa J. Haemoglobin Saint Louis β28(B10) Leucine→Glutamine. A new unstable haemoglobin only present in a ferri form. Abstract 408, XIV Intl. Cong. Hematol., Sao Paulo, 1972. FEBS Lett. 1973; 33: 37–41
   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) Leu→Gln. J. Clin. Invest. 1976; 58: 1098–1106
   PubMed Web of Science ®Google Scholar
• Sansone G., Carrell R. W., Lehmann H. Haemoglobin Genova: β28 (B10) Leucine→Proline. Nature 1967; 214: 877–879
   PubMed Web of Science ®Google Scholar
• Schmidt B., Bechtel K. C., Johnson M. H., Therrell B. J., Jr., Moo‐Penn W. F. Hemoglobin Lufkin: β29 (B11) Gly→Asp: An unstable hemoglobin variant involving an internal amino acid residue. Hemoglobin 1977; 1: 799–814
   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: 2125–2129
   PubMed Web of Science ®Google Scholar
• Jackson J. M., Yates A., Huehns E. R. Haemoglobin Perth: β32 (B14) Leu→Pro. An unstable haemoglobin causing haemolysis. Br. J. Haematol. 1973; 25: 607–610
   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) Leucines→Proline. An unstable variant producing severe hemolytic disease. J. Clin. Invest. 1973; 52: 1746–1755
   PubMed Web of Science ®Google Scholar
• Garel M. C., Blouquit Y., Rosa J. Hemoglobin Castilla β32(B14) Leu→Arg: A new unstable variant producing severe hemolytic disease. FEBS Lett. 1975; 58: 145–147
   Web of Science ®Google Scholar
• Rieder R. F., Oski F. A., Clegg J. B. Hemoglobin Philly (β35 Tyrosine→Phenylalanine): Studies in the molecular pathology of hemoglobin. J. Clin. Invest. 1969; 48: 1627–1642
   PubMed Web of Science ®Google Scholar
• Yaroaoka K. Hemoglobin Hirose: α1β2 37(C3) Tryptophan yield‐ing Serine. Blood 1971; 38: 730–738
   PubMed Web of Science ®Google Scholar
• Gacon G., Belkhodja O., Wajciuan H., Labie D. Structural and functional studies of Hb Rothchild β37 (C3) Trp→Arg. A new variant of the α1β2 contact. FEBS Lett. 1977; 82: 243–246
   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) Gln→Lys) and Hemoglobin Montgomery (α48 (CD6) Leu→Arg). Biochim. Biophys. Acta 1975; 379: 28–32
   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 α2β2 (39(C5) Gln→Glu), a mildly unstable variant found in a Finnish family. Hemoglobin 1977; 1: 292–295
   PubMed Web of Science ®Google Scholar
• Brown W. J., Niazi G. A., Jayalakshmi H., Abraham E. C., Huisman T. H. J. Hemoglobin Athens‐Georgia, or α2β2 40(C6) Arg→Lys, a hemoglobin variant with an increased oxygen affinity. Biochim. Biophys. Acta 1976; 439: 70–76
   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. Hemoglobins Austin and Waco: Two hemoglobins with substitutions in the α1β2 contact region. Arch. Biochem. Biophys. 1977; 179: 86–94
   PubMed Web of Science ®Google Scholar
• Burkett L. B., Sharma U. S., Pisciotta A. V., Ranney H. M., Bruckheimer S. Hemoglobin Meguon β41 (C7) Phenyl‐alanine→Tyrosine. Blood 1976; 48: 645–651
   PubMed Web of Science ®Google Scholar
• Dacie J. V., Shinton N. K., Gaffney P. J., Jr., Carrell R. W., Lehmann H. Haemoglobin Hammersmith (β42(CD1) Phe→Ser). Nature 1967; 216: 663–665
   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: 53–58
   PubMedGoogle Scholar
• Keeling M. M., Ogdon L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitchens J. L., Huisman T. H. J. Hemoglobin Louisville (β42(CDl)Phe→Leu): An unstable variant causing mild hemolytic anemia. J. Clin. Invest. 1971; 50: 2395–2402
   PubMed Web of Science ®Google Scholar
• Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemo‐globin Bucuresti β42(CD1) Phe→Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. Biophys. Acta 1971; 251: 1–6
   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: 193–199
   Web of Science ®Google Scholar
• Iuchi I., Ueda S., Hidaka K., Shibata S. Hemoglobin Hoshida (β43 (CD‐2) Glu→Gln), a new hemoglobin variant discovered in Japan. Hemoglobin 1978; 2: 235–247
   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: 658–661
   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 β‐chain variants of Haemoglobin A. Biochim. Biophys. Acta 1967; 140: 231–242
   PubMed Web of Science ®Google Scholar
• Marinucci M., Havilio F., Tentori L., Alberti R. Hemoglobin Gavello α2β2 47(CD6) Asp→Gly, a new hemoglobin variant from Polesine (Italy). Hemoglobin 1977; 1: 771–779
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Ala F. Haemoglobin Avicenna (β47 (CD6) Asp→Ala), a new abnormal haemoglobin. Biochim. Biophys. Acta 1979; 576: 466–470
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Milner P., Cobb L. Hemoglobin Okaloosa (β48(CD7) Leucine→Arginine). An unstable hemoglobin with decreased oxygen affinity. J. Clin. Invest. 1973; 52: 2858–2864
   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: 114–117
   PubMed Web of Science ®Google Scholar
• Jones R. T., Koler R. D., Duerst M. L., Dhindsa D. S. Hemoglobin Willamette [α2β2 51 Pro→Arg (D2)] a new abnormal human hemoglobin. Hemoglobin 1976; 1: 45–57
   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 acid→Asparagine) in combination with Haemoglobin S. J. Med. Genet. 1971; 8: 302–305
   PubMed Web of Science ®Google Scholar
• Beresford C. H., Clegg J. B., Weatherall D. J. Haemoglobin Ocho Rios (β52(D3) Aspartic acid→anine); a new β‐chain variant of Haemoglobin A found in combination with Haemoglobin S. J. Med. Genet. 1972; 9: 151–153
   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. J. Mol. Biol. 1966; 19: 91–108
   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: 732–738
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Lie‐Injo L. E., Pribadi W. Fast hemoglobin variant in Minahassan people of Sulawesi, Chinese and Thais: α2β2 56 Gly→Asp. Am. J. Phys. Anthropol. 1970; 32: 147–150
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Haydari H., Daneshmand P. Haemoglobin Hamadan α2β2 56 Glycine→Arginine (D7). Biochim. Biophys. Acta 1975; 379: 645–648
   PubMed Web of Science ®Google Scholar
• Giardina B., Brunori M., Antonini E., Tentori L. Properties of Hemoglobin G Ferrara (β57B(E1) Asn→Lys). Biochim. Biophys. Acta 1978; 534: 1–6
   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: 58–63
   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: 671–672
   Web of Science ®Google Scholar
• Blackwell R. Q., Tiu C. ‐S., Shih T. ‐B. Hemoglobin J Kaohsiung: β59 Lys→Thr. Biochim. Biophys. Acta 1971; 229: 343–348, β
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T. S., Liu C. ‐S., Weng H. ‐I., 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: 469–473
   PubMed Web of Science ®Google Scholar
• Wajcman H., Amegnizin K. P. E., Belkhodja O., Labie D. Hemoglobin J Lome β59(E3) Lys→Asn. A new fast moving variant found in a Togolese. FEBS Lett. 1977; 84: 372–374
   PubMed Web of Science ®Google Scholar
• Kagimoto T., Morino Y., Kishimoto S. A new hemoglobin variant Hb Yatsushiro αA2β602Val→Leu. Biochim. Biophys. Acta 1978; 532: 195–198
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huehns E. R., Motulsky A. G. Structural characterization of Hemoglobin N Seattle: α2Aβ2 61 Lys→Glu. Biochim. Biophys. Acta 1968; 154: 278–283
   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: 101–105
   PubMed Web of Science ®Google Scholar
• Beutler E., Lang A., Lehmann H. Hemoglobin Duarte: α2β2 62(E6) Ala→Pro: A new unstable hemoglobin with increased oxygen affinity. Blood 1974; 43: 527–535
   PubMed Web of Science ®Google Scholar
• Muller C. J., Kingma S. Haemoglobin Zürich α2Aβ263 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 H. Proc. Natl. Acad. Sci. USA 1961; 47: 1758–1767
   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: 486–494
   Google Scholar
• Murawski K., Szymanowska Z., Kozlowska J. A new variant of abnormal methaemoglobin: Hb M Radom. Biochim. Biophys. Acta 1963; 69: 442–444
   Web of Science ®Google Scholar
• Hobolth N., Haemoglobin M., Arhus I. Clinical family study. Acta Paediatr. Scand. 1965; 54: 357–362
   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: 918–925
   PubMed Web of Science ®Google Scholar
• Betke K., Gröschner E., Bock K. Properties of a further variant of Haemoglobin M. Nature 1960; 188: 864–865
   Web of Science ®Google Scholar
• Hörlein H., Weber G. Über chronishe familiäre methamo‐globinämie und eine neue modifikation des methämoglobins. Deutsche Medizinische Wochenschrift 1948; 73: 476–478
   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: 48–60
   PubMedGoogle Scholar
• Kohne E., Grosze H. P., Versmold H., Kley H. P., Kleihauer E. Hb M Erlangen: α2β2 63 (E7) Tyr. Eine neue mutation mit hämolyse und diaphorasemangel. Kinder‐heilk 1975; 120: 69–78
   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) His→Pro). J. Mól. Med. 1976; 1: 187–197
   Google Scholar
• Tentori L. Three examples of double heterozygosis beta‐ thalassemia and rare hemoglobin variants. Intl. Symp. Abnormal Hemoglobin and Thalassemia. Istanbul. Turkey 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) Lys→Asn, a beta homologue of Hb Zambia. FEBS Lett. 1974; 39: 200–204
   PubMed Web of Science ®Google Scholar
• Garel M. C., Hassan W., Coquelet M. T., Goossens M., Rosa J. Hemoglobin J Cairo: β65(E9) Lys→Gln, a new hemoglobin variant discovered in an Egyptian family. Biochim. Biophys. Acta 1976; 420: 97–104
   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) Lys→Glu: A new abnormal haemoglobin with a mutation localized on the E10 porphyrin surrounding zones. Nature 1969; 223: 190–191
   PubMed Web of Science ®Google Scholar
• Steadman J. H., Yates A., Huehns E. R. Idiopathic Heinz body anaemia: Hb‐Bristol (β67(E11) Val→Asp). Br. J. Haematol. 1970; 18: 435–446
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Lorkin P. A., Raik E., Hunter E. Haemoglobin Sydney: β67(E11) Valines‐Alanine: An emerging pattern of unstable haemoglobins. Nature 1967; 215: 626–628
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T. Hemoglobin Mizuho or beta 68(E12) Leucine→Proline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin 1977; 1: 467–477
   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: 836–840
   PubMedGoogle Scholar
• Kurachi S., Hermodson M., Hornung S., Stamatoyannopoulos G. Structure of Haemoglobin Seattle. Nature New Biol. 1973; 243: 275–276
   PubMedGoogle Scholar
• Carrell R. W., Owen M. C. A new approach to haemoglobin variant identification. Haemoglobin Christchurch β71(E15) Phenylalanine→Serine. Biochim. Biophys. Acta 1971; 236: 507–511
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Pootrakul S., Gray G. Hemo‐ globin Vancouver [α2β2 73(E17) Asp→Tyr]: Its structure and function. J. Mol. Evol. 1976; 9: 37–44
   PubMed Web of Science ®Google Scholar
• Konotey‐Abulu F. I. D., Gallo E., Lehmann H., Ringelhann B. Haemoglobin Korle‐Bu (β73 Aspartic acid‐Asparagine) showing one of the two amino acid substitutions of Haemoglobin C Harlem. J. Med. Genet. 1968; 5: 107–111
   PubMedGoogle Scholar
• Bio‐Doku F. S., Kinderlerer J., Lehmann H. Atlas of Protein Sequence and Structure 1972; 5: 73
   Google Scholar
• Schneider R. G., Hosty T. S., Tomlin G., Atkins R., Brimhall B., Jones R. T. Hb Mobile [α2β2 73(E17) Asp→Val]: A new variant. Biochem. Genet. 1975; 13: 411–415
   PubMed Web of Science ®Google Scholar
• Rieder R. F., Wolf D. J., Clegg J. B., Lee S. L. Rapid post‐synthetic destruction of unstable Haemoglobin Bushwick. Nature 1975; 254: 725–727
   PubMed Web of Science ®Google Scholar
• White J. M., Brain M. C., Lorkin P. A., Lehmann H., Smith M. Mild “unstable haemoglobin haemolytic anaemia” caused by Haemoglobin Shepherds Bush (β74 (E18) Gly→Asp). Nature 1970; 225: 939–941
   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 α2β2 75 Leu→Pro (E19): An unstable variant found in several members of a Caucasian family. Biochim. Biophys. Acta 1975; 386: 538–541
   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) Ala→Asp): A new hemoglobin variant resulting from a substitution of an external residue. Blood 1975; 45: 387–393
   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 His→Arg). Brit. Med. J. 1967; 1: 674–677
   PubMed Web of Science ®Google Scholar
• Blackuiell R. Q., Shih T. ‐B., Wang C. ‐L., Liu C. ‐S. Hemoglobin C‐Hsi‐Tsou: β79 Asp→Gly. Biochim. Biophys. Acta 1972; 257: 49–53
   PubMedGoogle Scholar
• Benesch R., Edilji R., Benesch R. E. Oxygenation proper‐ties 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 Asn→Lys. Biochim. Biophys. Acta 1969; 188: 59–64
   PubMed Web of Science ®Google Scholar
• Imai K., Morimoto H., Kotani H., Shibata S., Miyaji T., Hasutomo K. Studies on the function of abnormal hemoglobins. II. Oxygen equilibrium of abnormal hemoglobins: Shimonoseki, Ube II, Hikari, Gifu, and Agenogi. Biochim. Biophys. Acta 1970; 200: 197–202
   PubMedGoogle Scholar
• Schneider R. G., Hettig R. A., Bilunos H., Brimhall B. Hemoglobin Baylor [α2β2 81 (EF5) Leu→Arg]—an unstable mutant with high oxygen affinity. Hemoglobin 1976; 1: 85–96
   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., Bonaventura C. Hemoglobin Providence. A human hemoglobin variant occurring in two forms in vivo. J. Biol. Chem. 1976; 251: 7557–7562
   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: 7563–7571
   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 Lys→Thr): A new high affinity haemoglobin associated with decreased 2,3‐diphosphoglycerate binding and relative polycythaemia. Br. Med. J. 1975; 4: 200–202
   PubMed Web of Science ®Google Scholar
• Ikkala E., Koskela J., Pikkarainen P., Rahiala E. ‐L., El‐Hazmi M. A. F., Nagai 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] Lys→Met). Acta Haematol. 1976; 56: 257–75
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. ‐S., Wang C. ‐L. Hemoglobin Ta‐li: β83 Gly→Cys. Biochim. Biophys. Acta 1971; 243: 467–474
   PubMed Web of Science ®Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemo‐globin Pyrgos (α2β2 83(EF7) Gly→Asp). A new hemoglobin (Hb) variant. Annual Meeting of the American Society of Hematology. Miami 1972; 168
   Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemo‐globin Pyrgos α2β2 83(EF7) Gly→Asp: A new hemoglobin variant in double heterozygosity with Hemoglobin S. Blood 1976; 47: 827–832
   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 Phe→Ser, a new spontaneous mutation producing an unstable hemoglobin with high oxygen affinity. Annual Meeting of the American Society of Hematology. Miami 1972, Abstract 40
   Google Scholar
• de Weinstein B. I., White J. M., Wiltshire B. G., Lehmann H. A new unstable haemoglobin: Hb Buenos Aires, β85(F1) Phe→Ser. Acta Haematol. 1973; 50: 357–363
   PubMed Web of Science ®Google Scholar
• Watson‐Williams E. J., Beale D., Irvine D., Lehmann H. A new haemoglobin, D Ibadan (β87 Threonine→Lysine), producing no sickle cell Haemoglobin D disease with Haemoglobin S. Nature 1965; 205: 1273–1276
   PubMed Web of Science ®Google Scholar
• Hollender A., Lorkin P. A., Lehmann H., Svensson B. New unstable Haemoglobin Böras: β88(F4) Leucine→Arginine. Nature 1969; 222: 953–955
   PubMed Web of Science ®Google Scholar
• Opfell R. W., Lorkin P. A., Lehmann H. Hereditary non‐spherocytic haemolytic anaemia with post‐splenectomy inclusion bodies and pigmenturia caused by an unstable Haemoglobin Santa Ana—β88(F4) Leucine→Proline. J. Med. Genet. 1968; 5: 292–297
   PubMedGoogle Scholar
• Thillet J., Blouquit Y., Garel M. C., Dreyfus B., Reyes F., Cohen‐Solal M., Beuzard Y., Rosa J. Hemoglobin Creteil β89(F5) Ser→Asn: High oxygen affinity variant of hemoglobin frozen in a quaternary R‐structure. J. Mol. Med. 1976; 1: 135–150
   Google Scholar
• Paniker N. V., Kuang‐Tzu Davis Lin Krantz S.B., Flexner J. M., Wasserman B. K., Puett D. Haemoglobin Vanderbilt (α2β2 89 Ser→Arg): A new haemoglobin with high oxygen affinity and compensatory erythrocytosis. Br. J. Haematol. 1978; 39: 249–258
   PubMed Web of Science ®Google Scholar
• Miyaji R., Suzuki H., Ohba Y., Shibata S. Hemoglobin Agenogi (α2β2 90 Lys), a slow moving hemoglobin of a Japanese family resembling Hb‐E. Clin. Chim. Acta 1966; 14: 624–629
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Satoshi U., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sabine, β91(F7) Leu→Pro. An unstable variant causing severe anemia with inclusion bodies. N. Engl. J. Med. 1969; 280: 739–745
   PubMed Web of Science ®Google Scholar
• Ahern E., Ahem C., Hilton T., Serjeant G. R., Serjeant B. E., Seakins H., Lang A., Middleton A., Lehmann H. Haemoglobin Caribbean β91(F7) Leu→Arg: A mildly unstable haemoglobin with low oxygen affinity. FEBS Lett. 1976; 69: 99–102
   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: 311–329
   Google Scholar
• Beuzard Y., Courvalin J. Cl., Cohen‐Solal M., Garel M. C., Rosa J., Brizard C. P., Gibaud A. Structural studies of Hemoglobin Saint Etienne β92(F8) His→Gln: A new abnormal hemoglobin with loss of β proximal histidine and absence of heme on the β chains. FEBS Lett. 1972; 27: 76–80
   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., Müftuglü A. Hemoglobin Istanbul: Substitution of Glutamine for Histidine in a proximal Histidine (F8(92)β). J. Clin. Invest. 1972; 51: 2380–2387
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Przywara K. P., Shamsuddin M., Heller P. Hemoglobin J Altgeld Gardens (β92(F8) His→Asp): A new hemoglobin variant involving a substitution of the proximal histidine. Am. Soc. Hematol. 18th Annual Meeting. Dallas, Texas 1975
   Google Scholar
• Finney R., Casey R., Lehmann H., Walker W. Hb Newcastle: β92(F8) His→Pro. FEBS Lett. 1975; 60: 435–438
   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: 945–947
   PubMed Web of Science ®Google Scholar
• Gottlieb A. J., Robinson E. A., Itano H. A. Primary structure of Hopkins‐I haemoglobin. Nature 1967; 214: 189–190
   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 α2β2 95 Glu. Biochim. Biophys. Acta 1966; 117: 492–494
   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. Hemo‐globin Hiroshima (β143 Histidine→Aspartic 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: 525–535
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Schneider R. G., Andrian S., Das D. K. Hemoglobin Detroit: β95 (FG2) Lysine→Asparagine. Biochim. Biophys. Acta 1978; 536: 283–288
   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) Leu→Arg and Halmö: β97 (FG4) His→Gln. Biochem. J. 1970; 119: 68–74
   Web of Science ®Google Scholar
• Taketa F., Huang Y. P., Libnoch J. A., Dessell B. H. Hemoglobin Wood β97(FG4) His→Leu: A new high‐oxygen‐affinity hemoglobin associated with familial erythrocytosis. Biochim. Biophys. Acta 1975; 400: 348–353
   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: 3229–3233
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Hutchison H. E. Haemoglobin Köln (β98 Valines→Methionine): An unstable protein causing inclusion‐body anaemia. Nature 1966; 210: 915–916
   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., Hiyaji T., Shibata S. Identical substitution in Hb Ube‐1 and Hb Köln. Nature New Biol. 1973; 243: 205–207
   PubMedGoogle Scholar
• Gordon‐Smith E. C., Dacie J. V., Blecher T. E., French E. A., Wiltshire B. G., Lehmann H. Haemoglobin Nottingham, β98(FG5) Val→Gly: A new unstable haemoglobin producing severe haemolysis. Proc. Roy. Soc. Med. 1973; 66: 507–508
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. A new unstable hemo‐globin mutated in β98(FG5) Val→a: Hb Djelfa. FEBS Lett. 1975; 58: 238–240
   PubMed Web of Science ®Google Scholar
• Reed C. S., Hampson R., Gordon S., Jones R. T., Novy M. J., Brimhall B., Edwards H. J., Koler R. D. Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, Hemoglobin Kempsey. Blood 1968; 31: 623–632
   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: 1840–1847
   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 poly‐cythaeraia. Br. J. Haematol. 1977; 35: 177–191
   PubMed Web of Science ®Google Scholar
• Rueknagel 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. H. Hemoglobin Brigham (α2Aβ2 100 Pro→Leu). Hemoglobin variant associated with familial erythrocytosis. J. Clin. Invest. 1973; 52: 2060–2067
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Gray G. Hemoglobin British Columbia [α2β2 101(G3) Glu→Lys]: A new variant with high oxygen affinity. Hemoglobin 1976; 1: 171–182
   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: 261–269
   Web of Science ®Google Scholar
• Mant M. J., Salkie M. L., Cope N., Appling F., Bolch K., Jayalakshmi H., Gravely H., Wilson J. B., Huisman T. H. J. Hb Alberta or α2β2 (101(G3) Glu→Gly), a new high‐oxygen‐affinity hemoglobin variant causing erythrocytosis. Hemoglobin 1976; 1: 183–194
   PubMed Web of Science ®Google Scholar
• Charaćhe S., Jacobson R., Brimhall B., Murphy E. A., Hathaway P., Winslow R., Jones R., Rath C., Simkovich J. Hb Potomac (β101 Glu→Asp): Speculations on placental oxygen transport in carriers of high‐affinity hemoglobins. Blood 1978; 51: 331–338
   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: 6105–6116
   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: 980–991
   PubMed Web of Science ®Google Scholar
• Nagel R. L., Joshua L., Johnson J., Landau L., Bookchin R. H., Harris M. B. Hemoglobin Beth Israel: A mutant causing clinically apparent cyanosis. N. Engl. J. Med. 1976; 295: 125–130
   PubMed Web of Science ®Google Scholar
• White J. M., Szur L., Gillies I. D. S., Lorkin P. A., Lehmarm H. Familial polycythaemia caused by a new haemoglobin variant. Hb Heathrow β103(G5) Phenylalanines→Leucine. Br. Med. J. 1973; 3: 665–667
   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 haemo‐globin variant, Haemoglobin Camperdown β104(G6) Arginine→Serine. Biochim. Biophys. Acta 1975; 393: 195–200
   PubMed Web of Science ®Google Scholar
• Ryrie D. R., Plowman D., Lehmann H. Haemoglobin Sherwood Forest β104(G6) Arg→Thr. FEBS Lett. 1977; 83: 260–262
   PubMed Web of Science ®Google Scholar
• Hyde R. D., Hall M. D., Wiltshire B. G., Lehmann H. Haemoglobin Southampton, β106(G8) Leu→Pro: An unstable variant producing severe haemolysis. Lancet 1972; 2: 1170–1172
   PubMed Web of Science ®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) Leu→Pro, a contemporary mutation. Am. J. Med. 1973; 55: 549–558
   PubMed Web of Science ®Google Scholar
• Kleihauer E., Waller H. D., Benohr H. C., Kohne E., Gelinsky P. Hb Tübingen, eine neue β‐kettenvariante (βTp 10–12) mit erhöhter spontanozydation. Klin. Wochenschr. 1971; 48: 651–659
   Google Scholar
• Kohne E., Kley H. P., Kleihauer E., Versmold H., Benohr H. C., Braunitzer G. Structural and functional characteristics of the Hb Tübingen: β106(G8) Leu→Gln. FEBS Lett. 1976; 64: 443–447
   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)Gly→Arg]. Biochem. Gen. 1976; 14: 577–585
   PubMed Web of Science ®Google Scholar
• Imamura T., Fujita S., Ohta Y., Hanada M., Yanase T. Hemoglobin Yoshizuka (G10(108) β Asparagine→Aspartic acid): A new variant with a reduced oxygen affinity from a Japanese family. J. Clin. Invest. 1969; 48: 2341–2348
   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) Asparagine→Lysine. A hemoglobin variant with low oxygen affinity. FEBS Lett. 1978; 92: 53–56, α
   PubMed Web of Science ®Google Scholar
• Nute P. E., Stamatoyannopoulos G., Hermodson M. A., Roth D., Hornung S. Hemoglobinopathic erythrocytosis due to a new electrophoretically silent variant, Hemoglobin San Diego (β109(G11) Val→Met). J. Clin. Invest. 1974; 53: 320–328
   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 Deterborough, β111(G13) Valine→Phenylalanine, its interaction with normal haemoglobin and with Haemoglobin Lepore. Br. J. Haematol. 1972; 22: 125–134
   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: Post‐translational degradation of an unstable β‐chain variant producing a phenotype of severe heterozygous β‐thalassemia. Clin. Res. 1978; 26: 501A
   Google Scholar
• Ranney H. M., Jacobs A. S., Nagel R. L. Haemoglobin New York. Nature 1967; 213: 876–878
   PubMed Web of Science ®Google Scholar
• Outeirino J., Casey R., White J. M., Lehmann H. Haemo‐globin Madrid, β115(G17) Alanine→Proline: An unstable variant associated with haemolytic anaemia. Acta Haematol. 1974; 52: 53–60
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin P (α2β2 117Arg): Structure and properties. J. Lab. Clin. Med. 1969; 73: 616–622
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Berkman N. L., Brimhall B., Jones R. T. Hemoglobin Fannin‐Lubbock [α2β2119(GH2) Gly→Asp]: A slightly unstable mutant. Biochim. Biophys. Acta 1976; 453: 478–483
   PubMed 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 [α2β2119 (GH2) Gly→Asp]: A new hemoglobin variant at the α1β1 contact. Biochim. Biophys. Acta 1976; 453: 472–477
   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) Gly→Val. An electrophoretically silent variant migrating in isoelectrofocusing as Hb F. Hemoglobin 1979; 3: 253–262
   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: 204–206
   PubMedGoogle Scholar
• El‐Hazmi M. A. F., Lehmann H. Hemoglobin Riyadh [α2β2 120(GH3) Lys→Asn] ‐ a new variant found in association with α‐thalassemia and iron deficiency. Hemoglobin 1976; 1: 59–74
   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) Lysine→Asparagine. An example of Hb Riyadh in Japan. Hemoglobin 1977; 1: 461–466
   PubMed Web of Science ®Google Scholar
• Baglioni C. Abnormal human haemoglobins. VIII. Chemical studies on Haemoglobin D. Biochim. Biophys. Acta 1962; 59: 437–449
   PubMed Web of Science ®Google Scholar
• Ozsoylo S. Homozygous Hemoglobin D Punjab. Acta Haematol. 1970; 43: 353–359
   PubMed Web of Science ®Google Scholar
• Ramot B., Rotem J., Rahbar S., Jacobs A. S., Uden L., Ranney H. M. Hemoglobin D Punjab in a Bulgarian Jewish family. Israel J. Med. Sci. 1969; 5: 1066–1070
   PubMedGoogle Scholar
• Smith E. W., Conley C. L. Sickle cell‐Hemoglobin D disease. Ann. Intern. Med. 1959; 50: 94–98
   PubMed Web of Science ®Google Scholar
• Wasi P., Pootrakul S., Na‐Nakorn S., Beale D., Lehmann H. Haemoglobin D β Los Angeles (D Punjab, α2β2 121 GluNH2) in a Thai family. Acta Haematol. 1968; 39: 151–158
   PubMed Web of Science ®Google Scholar
• Imamura T., Riggs A. Identification of Hemoglobin Oak Ridge u/ith Hemoglobin D Punjab (Los Angeles). Biochem. Genet. 1972; 7: 127–130
   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: 569–573
   PubMed Web of Science ®Google Scholar
• Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229–232
   PubMed Web of Science ®Google Scholar
• Kamel K., Hoerman K., Awny A. Ethnological significance of hemoglobin α2β2 121 Lys. Am. J. Phys. Anthropol. 1970; 26: 107–108
   Web of Science ®Google Scholar
• Efremov G. D., Duma H., Rudivic R., Rolovic Z., Wilson J. B., Huisman T. H. J. Hemoglobin Beograd or α2β2 121 Glu→Val (GH4). Biochim. Biophys. Acta 1973; 328: 81–83
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Wong Hock Boon, Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 22: 379–380
   Web of Science ®Google Scholar
• Bursaux E., Blouguit Y., Poyart C., Rosa J., Arous N., Bohn B. Hemoglobin Ty Gard (αAβ2124(H2) Pro→Gln): A stable high O2 affinity variant at the α1β1, contact. FEBS Lett. 1978; 88: 155–159
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Takenaka H. Japanese haemoglobin variant. Nature 1968; 217: 89–90
   Web of Science ®Google Scholar
• Altay C., Altinöz N., Wilson J. B., Bolch K. C., Huisman T. H. J. Hemoglobin Hacettepe or α2β2 127 (H5) Gln→Glu. Biochim. Biophys. Acta 1976; 434: 1–3
   PubMed Web of Science ®Google Scholar
• Martinez G., Lima F., Colombo B. Haemoglobin J Guantanamo (α2β2 128 (H6) Ala→Asp). A new fast unstable haemoglobin found in a Cuban family. Biochim. Biophys. Acta 1977; 491: 1–6
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Yang Y. ‐J., Wang C. ‐C. Hemoglobin J Taichung: β129 Ala→Asp. Biochim. Biophys. Acta 1969; 194: 1–5
   PubMed Web of Science ®Google Scholar
• Maniatis A., Bousios T., Nagel R. L., Balazs T., Ueda Y., Bookchin R. H., Maniatis G. M. Hemoglobin Crete (β129 Ala→Pro): A new high‐affinity variant interacting with β° ‐ and δβ° ‐ thalassemia. Blood 1979; 54: 54–63
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Pietschmann H., Braunsteiner H., Lehmann H. Structure of Haemoglobin Wien β130 (H8) Tyrosine→Aspartic acid: An unstable haemoglobin variant. Acta Haematol. 1974; 51: 351–361
   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) Gln→Glu. Nature New Biol. 1973; 243: 467–468
   Google Scholar
• Ohba Y., Miyaji I., Matsuoka M., Ueda S., Iuchi I., Shibata S. Hemoglobin Tokuchi: β131 Glutamine→Glutamic acid, an example of Hb Camden in Japan. Acta Haematol. Jap 1975; 38: 1–7
   PubMedGoogle Scholar
• Brennan S. O., Arnold B., Fleming P., Carrell R. W. A new unstable haemoglobin, β1314 Val→Glu. Proc. New Zealand Med. J. 1977; 85: 398
   Google Scholar
• Arends T., Lehmarm H., Plowman D., Stathopoulou R. Haemoglobin North Shore‐Caracas β134 (H12) Valines→Glutamic acid. FEBS Lett. 1977; 80: 261–265
   PubMed Web of Science ®Google Scholar
• Marti H. R., Winterhalter K. H., Di Iorio E. E., Lorkin P. A., Lehmann H. Hb Altdorf α2β2 135(H13) Ala→Pro: A new electrophoretically silent unstable haemoglobin variant from Switzerland. FEBS Lett. 1976; 63: 193–196
   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: 830–838
   PubMed Web of Science ®Google Scholar
• Tentori L., Carta Sorcini M., Bucella C. Hemoglobin Abruzzo: Beta 143 (H21) His→Arg. Clin. Chim. Acta 1972; 38: 258–262
   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 His→Gln: (H21)). A high oxygen affinity haemoglobin variant with unique properties. Nature New Biol. 1973; 243: 177–179
   PubMedGoogle Scholar
• Jensen M., Oski F. A., Nathan D. G., Bunn H. F. Hemoglobin Syracuse (α2β2 143 (H21) His→Pro), a new high‐affinity variant detected by special electrophoretic methods. J. Clin. Invest. 1975; 55: 469–477
   PubMed Web of Science ®Google Scholar
• Zak S. J., Brimhall B., Jones R. T., Kaplan M. E. Hemo‐globin Andrew‐Minneapolis α2Aβ2 144 Lysr→Asn: A new high‐oxygen‐affinity mutant human hemoglobin. Blood 1974; 44: 543–549
   PubMed Web of Science ®Google Scholar
• Hayashim A., Stamatoyannopoulos G., Yoshida A., Adamson J. Haemoglobin Rainier: β145(HC2) tyrosine→Cysteine and Haemoglobin Bethesda: β145(HC2) Tyrosine→Histidine. Nature New Biol. 1971; 230: 264–267
   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 α2β2 145 Tyr→Asp, a new high‐oxygen‐affinity hemoglobin variant. Biochim. Biophys. Acta 1975; 400: 343–347
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Jones R. T. Polycythemia produced by Hemoglobin Osier (β145(HC2) Tyr→Asp). Johns Hopkins Med. J. 1975; 136: 132–136
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. Structural and functional study of Hb Nancy β145 (HC2) Tyr→Asp: A high oxygen affinity hemoglobin. FEBS Lett. 1975; 56: 39–42
   PubMedGoogle Scholar
• Winslow R. M., Swenberg M. ‐L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin Hckees Rocks (α2β2 145 Tyr→Term): A human “nonsense” mutation leading to a shortened β‐chain. J. Clin. Invest. 1976; 57: 772–781
   PubMed Web of Science ®Google Scholar
• Imai K. Oxygen‐Eguilibrium characteristics of abnormal Hemoglobin Hiroshima (α2β2 143 Asp). Arch. Biochem. Biophys. 1968; 127: 543–547
   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: 155–156
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kilmartin J. V., Najman A., Labie D. Hemoglobin Cochin‐Port Royal—conseguences of the replacement of the β chain C‐terminal by an arginine. Biochim. Biophys. Acta 1975; 400: 354–364
   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: 1406–1408
   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: 2057–2062
   PubMed Web of Science ®Google Scholar
• Ball E. W., Meynell M. J., Beale D., Kynach P., Lehmann H., Stretton A. O. W. Haemoglobin A2: α2δ2 16 Glycine→Arginine. Nature 1968; 209: 1217–1218
   Web of Science ®Google Scholar
• Rieder R. F., Clegg J. B., Weiss H. J., Christy N. P., Rabinowitz R. Hemoglobin A2‐Roosevelt: α2δ2 20 VaT→Glu. Biochim. Biophys. Acta 1976; 439: 501–504
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B. Structural characterization of two δ chain variants. J. Biol. Chem. 1967; 242: 5141–5145
   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 43Glu→Lys(CD2). Biochim. Biophys. Acta 1974; 359: 233–235
   PubMed Web of Science ®Google Scholar
• XIII Meeting Gruppo di Studio Dell'Entrocita, Torino, June, 121977
   Google Scholar
• Lie Injo L. E., Pribada W., Boerma F. W., Efremov G. D., Wilson J. B., Reynolds C. A., Huisman T. H. J. Hemoglobin A2‐Indonesia or α2δ2 69(E13) Gly→Arg. Biochim. Biophys. Acta 1971; 229: 335–342
   PubMedGoogle Scholar
• Sharma R. S., Williams L., Wilson J. B., Huisman T. H. J. Hemoglobin A2‐Coburg or α2δ2 116 Arg→His (G18). Biochim. Biophys. Acta 1975; 393: 379–382
   PubMed Web of Science ®Google Scholar
• DeJong W. W. W., Bernini L. F. Haemoglobin Babinga (δ136 Glycine→Aspartic acid): A new delta chain variant. Nature 1968; 219: 1360–1362
   PubMed Web of Science ®Google Scholar
• Lie‐Injo L. E., Kamuzora H., Lehmann H. Haemoglobin Malaysia: α2γ2 1(NA1) Glycines‐Cysteine: 136 Glycine. J. Med. Genet. 1974; 11: 25–30
   PubMed Web of Science ®Google Scholar
• Jenkins G. C., Beale D., Black A. J., Huntsman G. R., Lehmann H. Haemoglobin F Texas I (α2γ2 6Glu→Lys): A variant of Haemoglobin F. Br. J. Haematol. 1967; 13: 252–255
   PubMed Web of Science ®Google Scholar
• Ahern E. J., Wiltshire B. G., Lehmann H. Further character‐ization of Haemoglobin F. Texas I γ5 Glutamic acid→Lysine: γ136 Alanine. Biochim. Biophys. Acta 1972; 271: 61–64
   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 6Glu→Lys). The second of the Haemoglobin F Texas variants. Br. J. Haematol. 1968; 14: 233–238
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Owen M. C., Anderson R., Berry E. Haemoglobin F Auckland Gγ7 Asp→Asn—further evidence for multiple genes for the gamma chain. Biochim. Biophys. Acta 1974; 365: 323–327
   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: 114–118
   PubMed Web of Science ®Google Scholar
• Brannan S. O., Smith Merran B., Carrell R. W. Haemoglobin F Melbourne Gγ 16 Gly→Arg and Haemoglobin F Carlton Gγ 121 Glu→Lys. Biochim. Biophys. Acta 1977; 490: 452–455
   PubMedGoogle Scholar
• Lie‐Injo L. E., Wiltshire B. G., Lehmann H. Structural identification of Haemoglobin F Kuala Lumpur (α2γ2 22(B4) Asp→Gly: (136Ala). Biochim. Biophys. Acta 1973; 322: 224–230
   PubMed Web of Science ®Google Scholar
• Ahem E. J., Jones R. T., Brimhall B., Gray R. H. Haemoglobin F Jamaica (α2γ2 61 Lys→Glu: 136Ala). Br. J. Haematol. 1970; 18: 369–375
   PubMed Web of Science ®Google Scholar
• Ahem E., Holder W., Ahern V., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin F Victoria Jubilee (α2Aγ2 80 Asp→Tyr). Biochim. Biophys. Acta 1975; 393: 188–194
   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 9,000 Black and 7,000 White newborns: Haemoglobin F Dickinson (A97 His→Arg), a new variant. Br. J. Haematol. 1974; 28: 515–524
   PubMed Web of Science ®Google Scholar
• Omura H., Miyaji T., Shibata S. Hemoglobin F Ube (108 Asn→Lys), 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: 311–313
   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 acid→Lysine), homologous with Haemoglobins o and O Indonesia. Br. Med. J. 1967; 3: 531–533
   PubMed Web of Science ®Google Scholar
• Brimhall B., Vedvick T. S., Jones R. T., Ahern E., Palomino E., Ahern V. Haemoglobin F Port Royal (α2γ2 125 Glu→Ala). Br. J. Haematol. 1973; 27: 313–320
   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, α2Gγ2 130 Tryptophan→Glycine. J. Clin. Pathol. 1975; 28: 317–320
   PubMed Web of Science ®Google Scholar
• Barnabas J., Muller C. J. Haemoglobin Lepore Hollandia. Nature 1962; 194: 931–932
   Google Scholar
• Ostertag W., Smith E. W. Hemoglobin‐Lepore Baltimore, a third type of a δβ crossover (β50, β86). Eur. J. Biochem. 1969; 10: 371–376
   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: 1880–1886
   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. 1977; 234: 218–219
   Google Scholar
• Lehmann H., Charlesworth D. Observation on Haemoglobin P (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: 107–110
   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: 850–853
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Hilner P. F. Haemoglobin Constant Spring—a chain termination mutant. Nature 1971; 234: 337–340
   PubMed Web of Science ®Google Scholar
• Weatherall D. J., Clegg J. B. The α‐chain‐termination mutants and their relation to the α‐thalassemias. Phil. Trans. Roy. Soc. B 1975; 127: 411–455
   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: 245–247
   PubMed Web of Science ®Google Scholar
• DeJong W. W. W., Meera Khan P., Bernini L. F. Hemoglobin Koya Dora: High frequency of a chain termination mutant. Am. J. Hum. Genet. 1975; 27: 81–90
   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; 10: 732–733
   Google Scholar
• Imai K., Lehmann H. The oxygen affinity of Haemoglobin Tak, a variant with an elongated β chain. Biochim. Biophys. Acta 1975; 412: 288–294
   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: 119–131, Suppl
   Google Scholar
• Seid‐Akhaven H., Winter W. P., Abramson R. K., Rucknagel D. L. Hemoglobin Wayne: A frameshift variant occurring in two distinct forms. Ann. Mtg. Am. Soc. Hematol. Miami 1972, Abstract No. 9
   Google Scholar
• Bum H. F., Schmidt G. J., Haney D. N., Dluhy R. G. Hemoglobin Cranston, an unstable variant having an elongated β chain due to a non‐homologous crossover between two normal β chain genes. Proc. Natl. Acad. Sci. USA 1975; 72: 3609–3613
   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: 3270–3273
   PubMed Web of Science ®Google Scholar
• Tentori L. International Committee for Standardization in Hematology. KyotoJapan 1976, Personal communication
   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 α chain and oxygen equilibrium properties. Biochim. Biophys. Acta 1976; 453: 459–471
   PubMed Web of Science ®Google Scholar
• DeJong W. W. W., Went L. N., Bernini L. F. Haemoglobin Leiden: Deletion of β6 or 7 glutamic acid. Nature 1968; 220: 788–790
   PubMed Web of Science ®Google Scholar
• Cohen‐Solal M., Blouquit Y., Garel H. C., Thillet J., Gaillard L., Creyssel R., Gibaud A., Rosa J. Haemoglobin Lyon (β17–18(A14–15) Lys‐Val→O) determination of sequenator analysis. Biochim. Biophys. Acta 1974; 351: 306–316
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brirahall 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: 1024–1027
   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., Hiyaji T., Ueda S., Matsuoka H., Luchi 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: 440–445
   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: 495–504
   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: 1581–1583
   PubMed Web of Science ®Google Scholar
• Lutcher C. L., Huisman T. H. J. Hb‐Leslie, an unstable variant due to deletion of Gln β131, occurring in combination with β°‐thalassemia, Hb‐S, and Hb‐C. Clin. Res. 1975; 23: 278A, α
   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 β13(H9) occurring in associati on with β°‐thalassemia, Hb‐C., and Hb‐S. Blood 1976; 47: 99–112
   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) Glutamine deleted. Biochem. Biophys. Res. Commun. 1975; 65: 8–15
   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] Val→a) and Hb Coventry (β141[H19] Leu Deleted). Brit. J. Haematol. 1978; 38: 195–209
   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: 248–255
   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: 57–61
   PubMed Web of Science ®Google Scholar
• Adams J. G., Heller P. Hemoglobin Arlington Park (β6 Glu→Lys 95 Lys→Glu): Electrophoretically “silent” hemoglobin variant with two amino acid substitutions in the same polypeptide chain. Blood 1973; 42: 990
   Web of Science ®Google Scholar
• Blackwell R. Q., Wong Hock Boon, Liu C. ‐S., Weng M. I. Hemoglobin J Singapore: α78 Asn→Asp: α79 Ala→Gly. Biochim. Biophys. Acta 1972; 278: 482–490
   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) Glu→Val β58 (E2) Pro→Arg: The second sickling variant with amino acid substitutions in 2 residues of the β polypeptide chain. FEBS Lett. 1975; 58: 149–154
   PubMed Web of Science ®Google Scholar
• Hoo‐Penn W. F., Schmidt R. M., Jue D. L., Bechtel K. C., Wright J. M., Home M. K., III, Haycraft G. L., Roth E. F., Nagel R. L., Hemoglobin S Travis. A sickling hemoglobin with two amino acid substitutions [β6(A3) Glutamic acid→Valine and β142(H20) Alanine→Valine]. Eur. J. Biochem. 1977; 77: 561–566
   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 (α231(B12) Arg→Ser β2). Biochim. Biophys. Acta 1979; 578: 534–540
   PubMed Web of Science ®Google Scholar
• Abramov A., Lehmann H., Robb L. Hb Shaare Zedek (α56 E5 Lys→Glu). FEBS Letters 1980; 113: 235–237
   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)Leu+O]. Proc. Natl. Acad. Sci. USA 1981; 78: 469–473
   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(Bl) His→Tyr. Hemoglobin 1980; 4: 177–184
   PubMed Web of Science ®Google Scholar
• Tatsis B. Hemoglobin Queens (α34(B15) Leu→Arg): A new variant at the α1β1 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) Pro→Leu) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1980; 626: 424–431
   PubMed Web of Science ®Google Scholar
• Szelényi J. G., Horányi M., Fbldi J., Hudacsek J. István, Hollán S. R. A new hemoglobin variant in Hungary: Hb Savaria ‐ α49(CE7) Ser→Arg. Hemoglobin 1980; 4: 27–38
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Hatsuoka I. Hemoglobin Tottori (α59[E8] Glycine→Valine) a new unstable hemoglobin. Hemoglobin 1981; 5: 427–439
   PubMed Web of Science ®Google Scholar
• Spivak V. A., Molchanova T. P., Ermakov N. V., Tokarev Y. N., Martinez G., Szelenyi J., Horányi M., Foldi J., Hollán S., Kazieva H., Shamov I. A. A new hemoglobin variant: Hb Dagestan α60(E9) Lys→Glu. Hemoglobin 1981; 5: 133–138
   PubMed Web of Science ®Google Scholar
• Djoumessi S., Rousseaux J., Oescamps J., Goudemand M., Dautrevaux M. Hemoglobin Lille, α2 [74(EF3) Asp→Ala] β2. Hemoglobin 1981; 5: 475–479
   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) Asp→Ala, a new variant found in China. Hemoglobin 1981; 5: 481–486
   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[EF4] Asp→Gly): A new hemoglobin variant observed in a Japanese family. Hemoglobin 1980; 4: 209–214
   PubMed Web of Science ®Google Scholar
• Shibata S., Ueda S., Miyaji T., Imamura T. Hemoglobinopathies in Japan. Hemoglobin 1981; 5: 509–515
   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: 307–312
   PubMed Web of Science ®Google Scholar
• Honig G. R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschmann C. Hemoglobin Petah Tikva (α110 Ala→Asp): A new unstable variant with α‐thalassemia‐like expression. Blood 1981; 57: 705–711
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Hightower B., Carpentieri U., Duerst H. L., Shih T. B., Jones R. T. Hb Oleander [α116(GH4) Glu→Gln]: Structural and functional characterization. International Society of Haematology, European and African Division, Sixth Meeting, AthensGreece, August 30‐September 4, 1981
   Google Scholar
• Fleming P. J., Hughes W. G., Farmilo R. K., Wyatt K., Cooper W. N. Hemoglobin Westmead α2 122(H5) His→Gln β2: A new hemoglobin variant with the substitution in the α1β1, contact area. Hemoglobin 1980; 4: 39–52
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Iuchi I. Hemoglobin Yusa (β21(B3) Asp→Tyr), a new abnormal hemoglobin found in Japan. Hemoglobin 1981; 5: 121–131
   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) Asp→Gly): A hemoglobin variant with low oxygen affinity. Amer. J. Hemat. 1981; 11: 137–145
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Ohba Y. Abnormal hemoglobins in Japan. Hemoglobin 1980; 4: 395–408
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Braconnier F., Cohen‐Solal H., Foldi J., Arous N., Ankri A., Binet J. L., Rosa J. Hemoglobin Pitie‐Salpetriere β34(B16) Val→Phe a new high oxygen affinity variant associated with familial erythrocytosis. Biochim. Biophys. Acta 1980; 624: 473–478
   PubMed Web of Science ®Google Scholar
• Wilkinson T., Brennan S. O., Carrell R. W., Wells R. M., Como P., Kronenberg H. Hemoglobin Summer Hill β52 (D3) Asp→His a new variant from Sydney, Australia. Hemoglobin 1980; 4: 185–193
   PubMed Web of Science ®Google Scholar
• Marinucci M., Giuliani A., Maffi D., Massa A., Giampaolo A., Havilio F., Zannotti M., Tentori L. Hemoglobin Bologna (α2β2 61(E5) Lys→Het) an abnormal human hemoglobin with low oxygen affinity. Biochim. Biophys. Acta 1981; 668: 209–215
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Wells R. H., Smith H., Carrell R. W. Hemoglobin Brisbane: β68 Leu→His. A new high oxygen affinity variant. Hemoglobin 1981; 5: 325–335
   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) Leu→Arg: Identification by high performance liquid chromatography of a new unstable variant with increased oxygen affinity. Biochim. Biophys. Acta 1980; 623: 360–367, α
   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 acid→Tyrosine. Biochim. Biophys. Acta 1980; 623: 119–123
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Braconnier F., Galacteros F., Arous N., Soria J., Zittoun R., Rosa J. Hemoglobin Hotel‐Dieu β99 Asp→Gly (Gl). A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1981; 5: 19–31
   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 Takamatsu (β120 (GH3) Lys→Gln): A new abnormal hemoglobin detected in three unrelated families in the Takamatsu area of Shikoku. Hemoglobin 1980; 4: 165–176, α
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Jue D. T., 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: 347–361
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F., Schneider R. G., Shih T‐B., Jones R. T., Govindarajan S., Govindarajan P. G., Patchen L. C. Hemoglobin Ohio (β142 Ala→Asp): A new abnormal hemoglobin with high oxygen affinity and erythrocytosis. Blood 1980; 56: 246–250
   PubMed Web of Science ®Google Scholar
• Hirano M., Ohba Y., Imai K., Ino T., Morishita Y., Hatsui T., Shimizu S., Sumi H., Yamamoto K., Miyaji T. Hb Toyoake: β142(H20) Ala→Pro. A new unstable hemoglobin with high oxygen affinity. Blood 1981; 7: 697–704
   Google Scholar
• Schneider R. G., Bremner J. E., Brimhall B., Jones R. T., Shih T‐B. Hemoglobin Cowtown (β146 HC3 His→Leu) A mutant with high oxygen affinity and erythrocytosis. Amer. J. Clin. Pathol. 1979; 72: 1028–1032
   PubMed Web of Science ®Google Scholar
• Hayashi A., Fujita T., Fujimura M., Titani K. A new abnormal fetal hemoglobin, Hb FH‐Osaka (α2γ2 63 His→Tyr). Hemoglobin 1980; 4: 447–448
   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: 139–151
   PubMed Web of Science ®Google Scholar
• Adams J. G., III, Morrison W. T., Steinberg M. H. A double crossover within a single human gene: Hb Parchman (NH2—δβδ‐COOH). Am. Soc. Hum. Genet. Annual Mtg., Dallas, Oct., 28–311981
   Google Scholar
• Honig G. R., Shamsuddin M., Mason R. G., Vida L. N. Hemoglobin Lincoln Park: A γβ fusion (anti‐Lepore) variant with an amino acid deletion in the δ chain‐derived segment. Proc. Nat. Acad. Sci 1978; 75: 1475–1479
   PubMed Web of Science ®Google Scholar
• Rahbar S., Winkler K., Louis J., Rea C., Blume K., Beutler E. Hemoglobin Great Lakes (β68[E12] Leucine→Histidine): A new high‐affinity hemoglobin. Blood. 1981; 58: 813–817
   PubMed Web of Science ®Google Scholar
• Lee‐Potter J. P., Deacon‐Smith R. A., Lehmann H., Robb L. Haemoglobin Ferndown (α6[A4] Aspartic acid→Valine). FEBS Lett. 1981; 126: 117–119
   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) Lys→Gln β2. Hemoglobin 1981; 5: 679–687
   PubMed Web of Science ®Google Scholar
• Liang C., Tao H., Lo H., Huang S., Li R., Wang B. Hemoglobin Shuangfeng (α27(B8)Glu→Lys): A new unstable hemoglobin variant. Hemoglobin 1981; 5: 691–700
   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)Pro→Arg]: A new hemoglobin variant of high oxygen affinity with amino acid substitution at α1β1 contact. Hemoglobin 1982; 6: 43–49
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hb Handa [α90(FG2)Lys→Met]: Structure and biosynthesis of a new slightly higher oxygen affinity variant. Hemoglobin, 6, In press
   Web of Science ®Google Scholar
• Goossens H., Lee K. Y., Liebhaber S. A., Kan Y. W. Globin structural mutant α125Leu→Pro is a novel cause of α‐thalassaemia. Nature 1982; 296: 864–865
   PubMed Web of Science ®Google Scholar
• Djoumessi S., Rousseaux J., Dautrevaux M. Structural studies of a new hemoglobin: Hb J Lens, β13(A10) Ala→Asp. FEBS Lett. 1981; 136: 145–147
   PubMed Web of Science ®Google Scholar
• Boissel J. P., Wajcman H., Fabritius H., Cabannes R., Labie D. Application of high‐performance liguid 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: 203–206
   PubMed Web of Science ®Google Scholar
• Nakatauji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., Shinohara T., Hori T., Takayama J. Hemoglobin Miyashiro (β23[B5] Val→Gly) an electrophoreti‐cally silent variant discovered by the isopropanol test. Hemoglobin 1981; 5: 653–666
   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)Leu→Pro, causing hemolytic anemia. Hemoglobin 1981; 5: 667–678
   PubMed Web of Science ®Google Scholar
• Moo‐Penn W. F. 1981, Reported International Society Haematology
   Google Scholar
• Spivak V. A., Holchanova T. P., Postnikov Y. V., Aseeva E. A., Lutsenko I. N., Tokarev Y. N. A new abnormal hemoglobin: Hb Mozhaisk β92(F8)His→Arg. Hemoglobin 1982; 6: 169–181
   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 94Asp(FG1)→His). J. Mol. Biol. 1982; 156: 185–202
   PubMed Web of Science ®Google Scholar
• Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., Chevrier M., Bordahandy C., Rosa J. Hemoglobin Saint Mandé β102(G4)Asn→Tyr: A new low oxygen affinity variant. FEBS Lett. 1981; 126: 114–116
   PubMed Web of Science ®Google Scholar
• Gibb E. A., Rucknagel D. L. 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. Hb F‐Meinohama or α2β2 (5 Glu→Gly; 75Ile; 136Gly). Hemoglobin 1981; 5: 565–570
   PubMed Web of Science ®Google Scholar
• Yoshinaka H., Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K. A new γ chain variant, Hb F Kotobuki or AγI6 (A3) Glu→Gly. Hemoglobin 1982; 6: 37–42
   PubMed Web of Science ®Google Scholar
• Johnson C. S., Schroeder W. A., Shelton J. B., Shelton J. R. Hemoglobin Boyle Heights: The first example of a deletion in the α chain. Blood 1981; 58(Suppl. 1)#5
   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: 45–48
   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 isoleucine→Threonine at position 75 (E19) of the γ chain. Hum. Genet. 1976; 32: 305–313
   PubMed Web of Science ®Google Scholar
• Webber B. B., Lam H., Wilson J. B., Huisman T. H. J. Hb Albany‐Ga or α211(A9)Lys→Asn β2. Hemoglobin 1983; 7, in press
   Google Scholar
• Honig G. R., Shamsuddin M., Vida L. N., Mompoint M., Bowie L., Jones E., Weil S. Hb Evanston (α14 Trp→Arg): 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)Lys→Asn]: A New Fast‐Moving Hemoglobin Variant. Hemoglobin 1982; 6(6)629–633
   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 His→Gln. FEBS Letters 1983; 145(1)128–130
   Web of Science ®Google Scholar
• Zeng Y. ‐T., Huang S. ‐Z., Zhou X. ‐D., Qiu X. ‐K., Dong Q. ‐y., Li M. ‐y., Bai J. ‐h. Hb Shenyang [α26(B7)Ala→Glu]: A New Unstable Variant Found in China. Hemoglobin 1982; 6(6)625–628
   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)Asn→Lys 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 [αl39(HC1)Lys→Thr]: A New Hemoglobin Variant with a Slightly Increased Oxygen Affinity. Hemoglobin 1983; 7(1)85–90
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Imai K., Seki M. Hemoglobin Machida [β6(A3)Glu→Gln], A New Abnormal Hemoglobin Discovered in a Japanese Family: Structure, Function and Biosynthesis. Hemoglobin 1982; 6(5)531–535
   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)Lys→Thr] A New Variant Found in a Mexican‐American Family. Hemoglobin 1983; 7(1)91–95
   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. Hematol. 1979; 21(4)347–352
   PubMedGoogle Scholar
• Brennan S. O., Williamson D., Whisson M. E., Carrell R. W. Hemoglobin Palmerston North β23(B5)Val→Phe A New Variant Identified in a Patient with Polycythemia. Hemoglobin 1982; 6(6)596–575
   Web of Science ®Google Scholar
• Arous N., Galacteros F., Fessas Ph., Loukopoulos D., Blouquit Y., Komis G., Sellaye M., Boussiou M. F., Rosa J. Structural Study of Hemoglobin Knossos, β27(B9)Ala→Ser. A New Abnormal Hemoglobin Present as a Silent β‐Thalassemia. FEBS Letters 1982; 147: 247–250
   PubMed Web of Science ®Google Scholar
• Boissel J. P., Wajcman H., Labie D., Fabritius H., Cabannes R. Hb J Daloa [β57(E1)Asn→Asp]: A New Variant Found in Ivory Coast. Hemoglobin 1982; 6(4)433–437
   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)Asp→Asn]. Hemoglobin 1983; 7, in press
   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) His→Pro, a New Variant Causing Hemolytic Disease. Hemoglobin 1983; 7(1)47–56
   PubMed Web of Science ®Google Scholar
• Lu Y. ‐Q., Feng J. ‐L., Liu J. ‐F, Hu H. ‐L, Peng X. ‐H., Huang P. ‐Y., Chen S. ‐S., Jia P. ‐C., Yang K. ‐C., Liang C. ‐C., Ren X. ‐D., Zuo C. ‐R. Hemoglobin Jianghua [β120(GH3)Lys→Ile]: A New Fast‐Moving Variant Found in China. Hemoglobin 1983; 7, in press
   PubMed Web of Science ®Google Scholar
• Yang K., Chen S., Jia P., Ma Y., Wu S., Liang C., Chen X., Zhang M., Tu I., Gong S. Hemoglobin Jinan [β139(H17)Asn→Asp), A New Abnormal Hemoglobin Found in China. Hemoglobin 1983; 7, in press
   PubMedGoogle Scholar
• Salkie M. L., Gordon P. A., Ringal W. M., Lam H., Wilson J. B., Headlee M. E., Huisman T. H. J. Hb A2 ‐Canada or α2β2 99(G1)Asp→Asn, A Newly Discovered Delta Chain Variant with Increased Oxygen Affinity Occurring In Cis to β‐Thal‐assemia. Hemoglobin 1982; 6(3)223–231
   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)Glrn→Glu in Association with δβg‐Thalassemia in a Yugoslavian Female. Hemoglobin 1983; 7, in press
   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 γ Chain Variant: Hb F‐Pordenone [γ6(A3)Glu→Gln: 75Ile: 136Ala]. Hemoglobin 1982; 6(4)397–401
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Headlee M., Lam H., Wilson J. B., Huisman T. H. J. Hb F‐Bonaire‐Ga or α2Aβ239(C5)Gln→Arg, Characterized by High Pressure Liguid Chromatographic and Microseguencing Procedures. Hemoglobin 1982; 6(6)599–606
   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 Ser→Arg); A Newly Identified Variant From an American Infant of Polish Descent. Bicchimica Biophysica Acta 1982; 707: 213–216
   PubMed Web of Science ®Google Scholar
• Serjeant G. R., Serjeant B. E., Lehmann H., Dukes M., Robb L. Hb F Kingston [Gγ55(D6)Met→Arg]. FEBS Letters 1982; 130(1)77–80
   Google Scholar
• Nakatsuji T., Lam H., Huisman T. H. J. Hb F‐Kennestone orα2Gγ2 (EF‐1)77 His→Arg Observed in a Caucasian Baby. Hemoglobin 1983; 2, in press
   Google Scholar
• Nakatsuki T., Lam H., Carver J., Huisman T. H. J. Hb F‐Marietta or GγI80[FF 4‐]Asp→Asn, Observed in a Caucasian Baby. Hemoglobin 1982; 6(4)407–411
   PubMedGoogle Scholar
• Nakatsuii T., Lam H., Wilson J. B., Webber B. B., Huisman T. H. J. Hb F‐Columbus‐Ga α2Gγ2 94(FGl)Asp→Asn. Hemoglobin 1982; 6(6)593–598
   PubMedGoogle Scholar
• Shelton J. B., Shelton J. R., Espinueva Z., Huynh V., Schroeder W. A., Powars D. Hemoglobin F‐Caltech: α2Gγ2120Lys→Gln. Hemoglobin 1982; 6(6)577–592
   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) Gly→Lys]. A New Fetal Hemoglobin Variant. Hemoglobin 1983; 7(1)79–83
   PubMed Web of Science ®Google Scholar
• Honig G. R. 1982, personal communication
   Google Scholar
• Bradley T. B. 1982, personal communication
   Google Scholar