Advanced search
Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 21, 1997 - Issue 6
Submit an article Journal homepage
40
Views
5
CrossRef citations to date
0
Altmetric
Miscellaneous Article

International Hemoglobin Information Center Variant List

M. F. H. Carver Research & Education Building, Room CB-2208 Medical College of Georgia, Augusta, GA, 30912-2110, USA
&
T. H. J. Huisman Research & Education Building, Room CB-2208 Medical College of Georgia, Augusta, GA, 30912-2110, USA
Pages 505-506 | Published online: 07 Jul 2009

References

  • Crookston J. H., Beale D., Irvine D., Lehmann H. A new Haemoglobin J Toronto (α5 Alanine→Aspartic acid). Nature 1965; 208: 1059
  • Sumida I., Ohta Y., Imamura T., Yanase T. Hemoglobin Sawara: α6(A4) Aspartic acid & Alanine. Biochim. Biophys. Acta 1973; 322: 23
  • Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M. Increased oxygen affinity for Hemoglobin Sawara: αA4(6) Aspartic acid→Alanine. Biochim. Biophys. Acta 1977; 495: 183
  • Jue D. L., Johnson M. H., Patchen L. C., Moo-Penn W. F. Hemoglobin Dunn: α6(A4) Aspartic acid→Asparagine. Hemoglobin 1979; 3: 137
  • Pootrakul S., Kematorn B., Na-Nakorn S., Suanpan S. A new α hemoglobin variant: Haemoglobin Anantharaj alpha 11 (A9) Lysine→Glutamic acid. Biochim. Biophys. Acta 1975; 405: 161
  • Rosa J., Maleknia N., Vergoz D., Dunet R. Une nouvelle hemoglobine anormale: I'hemoglobin J α Paris 12 Ala→Asp. Nouv. Rev. Fr. d'Hematol. 1965; 6: 423
  • Trincao C., Martins DeMelo J., Lorkin P. A., Lehmann H. Haemoglobin J Paris in the South of Portugal (Algarve). Acta Haematol. 1968; 39: 291
  • Marti H. R., Pik C., Mosimann P. Eine neue hämoglobin I variante: Hb I Interlaken. Acta Haematol. 1964; 32: 9
  • Liddell J., Brown D., Beale D., Lehmann H., Huntsman R. G. A new haemoglobin - J Oxford found during a survey of an English population. Nature 1964; 204: 269
  • Silvestroni E., Bianco I., Tentori L., Vivaldi G., Carta S., Sorcini M., Brancati C. (1967) The structural abnormality of Hemoglobin N present in a family from Cosenza. Proceedings of the 10th Congress of the European Society of Hematology, Strasbourg, 1965. Karger, Basel/New York, 232, Part II
  • 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
  • Pootrakul S., Srichiyanont S., Wasi P., Suanpan S. Hemoglobin Siam α2 15 Arg β2): A new α chain variant. Humangenetik 1974; 23: 199
  • Beale D., Lehmann H. Abnormal haemoglobins and the genetic code. Nature 1965; 207: 259
  • Schneider R. G., Alperin I. B., Beale D., Lehmann H. Hemoglobin I in an American Negro family: Structural and hematologic studies. J. Lab. Clin. Med. 1966; 68: 940
  • Bowman B. H., Barnett D. R. Amino-acid substitution in Haemoglobin I (Texas variant). Nature 1967; 214: 499
  • 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
  • Baur E. W. Hb α2 glu β2 (Hb I) in a Caucasian family: Independent mutation or common origin. Humangenetik 1968; 6: 368
  • 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
  • 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-Kurosh [α19 (AB1) Ala→Asp]. Biochim. Biophys. Acta 1976; 427: 119
  • Kendall A. G., Barr R. D., Lang A., Lehmann H. Haemoglobin J Nyanza: α21 (B2) Ala→Asp. Biochim. Biophys. Acta 1973; 310: 357
  • Gottlieb A. J., Restrepo A., Itano H. A. Hemoglobin J Medellin. Chemical and genetic study. Fed. Proc 1964; 23: 172
  • 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 (α23GluNH2). J. Lab. Clin. Med. 1965; 66: 886
  • Boyer S. H., Crosby E. F., Fuller G. F., Ulenurm L., Buck A. A. A survey of hemoglobins in the Republic of Chad and characterization of Hemoglobin Chad. α2 23 Glu→Lys β2. Am. J. Hum. Genet. 1968; 20: 570
  • 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
  • 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
  • Ahem E., Ahern V., Holder W., Palomino E., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin Spanish Town α27 Glu→Val (B8). Biochim. Biophys. Acta 1976; 427: 530
  • Vettore L., DeSandre G., Dilorio E. E., Winterhalter K. H., Lang A., Lehmann H. A new abnormal hemoglobin O Padova, α30 (B11) Glu→Lys and a dyserythropoietic anemia with erythroblastic multinuclearity co-existing in the same patient. Blood 1974; 44: 869
  • Schneider R. G., Jim R. T.S. A new haemoglobin variant (the ‘Honolulu Type’) in a Chinese. Nature 1961; 190: 454
  • Vella F., Ager J. A. M., Lehmann H. An abnormal haemoglobin in a Chinese: Haemoglobin G. Nature 1958; 182: 460
  • 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
  • Marinucci M., Mavilio F., Tentori L., D'Erasmo F., Colapietro A., De Stasio G., Di Fonzo S. A new human hemoglobin variant: Hb Ban (α2 45(CD3) His→Gln β2). Biochim. Biophys. Acta 1980; 622: 315
  • Beretta A., Prato V., Gallo E., Lehmann H. Haemoglobin Torino - α43 (CD1) Phenylalanine→'Valine. Nature 1968; 217: 1016
  • Ohba Y., Miyaji T., Matsouka M., Yokoyama M., Numakura H., Nagata K., Takebe Y., Izumi Y., Shibata S. Hemoglobin Hirosaki (α43 [CE1] Phe→Leu), a new unstable variant. Biochim. Biophys. Acta 1975; 405: 155
  • 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
  • Sumida I. Studies of abnormal hemoglobins in Western Japan. Frequency of visible hemoglobin variants, and chemical characterization of Hemoglobin Sawara (α26Ala β2) and Hemoglobin Mugino (Hb L Ferrara; α247Glyβ2). Jap. J. Hum. Genet. 1975; 19: 343
  • 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
  • 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
  • Halbrecht I., Isaacs W. A., Lehmann H., Ben-Porat F. Hemoglobin Hasharon (α47 Aspartic acid→Histidine). Israel J. Med. Sci. 1967; 3: 827
  • Ostertag W., Smith E. W. Hb Sinai: A new a chain mutant α47 His. Humangenetik 1968; 6: 377
  • Schneider R. G., Ueda S., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sealy (α2 47His β2): A new variant in a Jewish family. Am. J. Hum. Genet. 1968; 20: 151
  • Bianco I., Modiano G., Bottini E., Lucci R. Alteration in the α-chain of Haemoglobin L Ferrara. Nature 1963; 198: 395
  • Tentori L. Hemoglobin L Ferrara = Hemoglobin Hasharon. Hemoglobin 1977; 1: 602
  • Rahbar S., Mahdavi N., Nowzari G., Mostafavi I. Hemoglobin Arya α2 47(CD5) Aspartic acid→Asparagine. Biochim. Biophys. Acta 1975; 386: 525
  • 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
  • Tangheroni W., Zorcolo G., Gallo E., Lehmann H. Haemoglobin J Sardegna: α50 (CD8) Histidine→Aspartic acid. Nature 1968; 218: 470
  • Cabannes R., Renaud R., Mauran A., Pennors H., Charlesworth D., Price B. G., Lehmann H. Deux hemoglobines rapides an Cote-D'Ivoire: I'Hb K Woolwich et une nouvelle hemoglobine, I'Hb J Abidjan (α51 Gly→Asp). Nouv. Rev. Fr. d'Hematol. 1972; 12: 289
  • Reynolds C. A., Huisman T. H.J. Hemoglobin Russ or α2 51 Arg β2. Biochim. Biophys. Acta 1966; 130: 541
  • 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
  • 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
  • Jones R. T., Brimhall B., Lisker R. Chemical characterization of Hemoglobin Mexico and Hemoglobin Chiapas. Biochim. Biophys. Acta 1968; 154: 488
  • Rosa J., Labie D., Maleknia N., Blum N. Sur quelques hemoglobines anormales nouvelles recemment isolees en France. International Symposium on Comparative Hemoglobin Structure, Thessaloniki, 1966, 140
  • Fessas Ph., Kaltsoya A., Loukopoulos D., Nilsson L.-O. On the chemical structure of Haemoglobin Uppsala. Hum. Hered. 1969; 19: 152
  • 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
  • Rahbar S., Kinderlerer J. L., Lehmann H. Haemoglobin L Persian Gulf: α57 (E6) Glycine→Arginine. Acta Haematol. 1969; 42: 169
  • Baglioni C. A chemical study of Hemoglobin Norfolk. J. Biol. Chem. 1962; 237: 69
  • Imamura T. Hemoglobin Kagoshima: An example of Hemoglobin Norfolk in a Japanese family. Am. J. Hum. Genet. 1966; 18: 584
  • 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
  • Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl. Acad. Sci., USA 1961; 47: 1758
  • 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
  • Hansen H. A., Jagenburg O. R., Johansson B. G. Studies on an abnormal hemoglobin causing hereditary congenital cyanosis. Acta Paediatr. 1960; 49: 503
  • Hollan S. R., Szelenyi J. G., Lehmann H., Beale D. A Boston-type Haemoglobin M in Hungary: Haemoglobin M Kiskunhalas. Haematologia 1967; 1: 11
  • Barclay G. P. T., Charlesworth D., Lehmann H. Abnormal haemoglobin in Zambia. A new Haemoglobin Zambia α60 (E9) Lysine→Asparagine. Br. Med. J. 1969; 4: 595
  • 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
  • Thillet J., Blouquit Y., Perrone F., Rosa J. Hemoglobin Pontoise α63 Ala→Asp (E12). A new fast moving variant. Biochim. Biophys. Acta 1977; 491: 16
  • 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
  • Ramot B., Kinderlerer J. B., Lehmann H. Cited in WHO Technical Report Series No. 509. Annex 1, Geneva, 1972
  • 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
  • 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
  • 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
  • Chemoff 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
  • Bowman B., Barnett D. R., Hodgkinson K. T., Schneider R. G. Chemical characterization of Haemoglobin G St-1. Nature 1966; 211: 1305
  • 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
  • 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
  • Colombo B., Vidal H., Kamuzora H., Lehmann H. A new Haemoglobin J-Habana α71 (E20) Alanine→Glutamic acid. Biochim. Biophys. Acta 1974; 351: 1
  • Rahbar S., Nowzari G., Daneshmand P. Hemoglobin Daneshgah Tehran α2 72 (EF1) Histidine→Arginine β2A. Nature New Biol. 1973; 245: 268
  • Pootrakul S., Dixon G. H. Hemoglobin Mahidol: A new hemoglobin α-chain mutant. Can. J. Biochem. 1970; 48: 1066
  • Blackwell R. Q., Liu C.-S. Hemoglobin G Taichung: α74 Asp→His. Biochim. Biophys. Acta 1970; 200: 70
  • 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
  • Oninger E. P., Wilson J. B., Huisman T. H.J. Hemoglobin Chapel Hill or α2 74 Asp→Gly β2. FEBS Lett. 1976; 65: 297
  • Vella F., Wiltshire B., Lehmann H., Galbraith P. Hemoglobin Winnipeg α2 75 Asp→Tyr β2. Clin. Biochem. 1973; 6: 66
  • Ohba Y., Miyaji T., Matsuoka M., Takeda I., Fukuba Y., Shibata S., Ohkura K. Hemoglobin Matsue-Oki: alpha 75 (EF4) Aspartic acid→Asparagine. Hemoglobin 1977; 1: 383
  • Van Ros G., Beale D., Lehmann H. Haemoglobin Stanleyville-11 (α78 Asparagine→Lysine). Br. Med. J. 1968; 4: 92
  • Rucknagel D. L., Brandt N. J., Spencer H. H. α-Chain mutants of human hemoglobin contributing to the genetics of the α-chain locus. Proceedings of the 1st Inter-American Symposium on Hemoglobins, Caracas, 1969
  • 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
  • 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 a sickle hemoglobin. Blood 1978; 52: 113, (Suppl. 1)
  • 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
  • Crookston J. H., Farquharson H. A., Beale D., Lehmann H. Hemoglobin Etobicoke: α84 (F5) Serine replaced by Arginine. Can. J. Biochem. 1969; 47: 143
  • Huehns E. R. The unstable hemoglobins. Bull. Soc. Chem. Biol. 1970; 52: 1131
  • 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
  • Cohen-Solal M., Manasse B., Thillet J., Rosa J. Haemoglobin G Norfolk α85 (F6) Asp→Asn. Structural characterization by sequenator analysis and functional properties of a new variant with high oxygen affinity. FEBS Lett. 1975; 50: 163
  • 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
  • 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
  • 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
  • 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
  • Heller P., Weinstein H. G., Yakulis V. J., Rosenthal I. M. Hemoglobin M Kankakee, a new variant of Hemoglobin M. Blood 1962; 20: 287
  • Pik C., Tonz O. Nature of Haemoglobin M Oldenburg. Nature 1966; 210: 1182
  • De Traverse P. M., Lehmann H., Coquelet M. L., Beale D., Isaacs W. A. Etude d'une hemoglobine J α non encore decrite, dans une famille Francaise. Compt. R. Sceanc. Soc. Biol. 1966; 160: 2270
  • Vella F., Charlesworth D., Lorkin P. A., Lehmann H. Hemoglobin Broussais α90 Lys→Asn. Can. J. Biochem. 1970; 48: 908
  • Braconnier F., Cohen-Solal M., 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'Hematol 1975; 15: 333
  • Hyde R. D., Kinderlerer J. L., Lehmann H., Hall M. D. Haemoglobin J Rajappen: α90 (FG2) Lys→Thr. Biochim. Biophys. Acta 1971; 243: 515
  • 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
  • Botha M. C., Beale D., Isaacs W. A., Lehmann H. Haemoglobin J Cape Town α2 92 Arginine→Glutamine β2. Nature 1966; 212: 792
  • Lines J. G., McIntosh R. Oxygen binding by Haemoglobin J Cape Town (α2 92 Arg→Gln). Nature 1967; 215: 297
  • Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol 1966; 19: 91
  • Charache S., Weatherall D. J., Clegg J. B. Polycythemia associated with a hemoglobinopathy. J. Clin. Invest. 1966; 45: 813
  • Wajeman H., Belkhodja O., Labie D. Hb Setif: G1(94) αAsp→Tyr. A new a chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits. FEBS Lett. 1972; 27: 298
  • Schneider R. G., Atkins R. J., Hosty T. S., Tomlin G., Casey R., Lehmann H., Lorkin P. A., Nagai K. Haemoglobin Titusville: α94 Asp→Asn, a new haemoglobin with a lowered affinity for oxygen. Biochim. Biophys. Acta 1975; 400: 365
  • Schroeder W. A., Shelton J. B., Shelton J. R., Powars D. Hemoglobin Sunshine Seth - α2 (94(G1) Asp→His) β2. Hemoglobin 1979; 3: 145
  • Huisman T. H. J., Adams H. R., Wilson J. B., Efremov G. D., Reynolds C. A., Wrightstone R. N. Hemoglobin G Georgia or α2 β2. Biochim. Biophys. Acta 1970; 200: 578
  • 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
  • De Jong W. W. W., Bernini L. F., Meera Khan P. Haemoglobin Rampa: α95 Pro→Ser. Biochim. Biophys. Acta 1971; 236: 197
  • Wiltshire B. G., Clark K. G. A., Lorkin P. A., Lehmann H. Haemoglobin Denmark Hill α95 (G2) Pro→Ala, a variant with unusual electrophoretic and oxygen binding properties. Biochim. Biophys. Acta 1972; 278: 459
  • 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
  • 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
  • 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
  • Charache S., Ostertag W., Von Ehrenstein G. Clinical studies and physiological properties of Hopkins-2 haemoglobin. Nature New Biol. 1971; 234: 248
  • Clegg J. B., Charache S. The structure of Hemoglobin Hopkins-2. Hemoglobin 1978; 2: 85
  • 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-1 α2 12 (A10) Ala→Asp β2 in the same population.). Biochim. Biophys. Acta 1975; 412: 181
  • 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
  • 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
  • Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229
  • Lie-Injo L. E., Sadono. Haemoglobin O (Buginese X) in Sulawesi. Br. Med. J. 1958; 1: 1461
  • 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)
  • Ohba Y., Miyaji T., Matsuoka M., Morito M., Iuchi I. Characterization of Hb Ube-4: Alpha 116 (GH4) Glu→Ala. Hemoglobin 1978; 2: 181
  • Blackwell R. Q., Wong H. B., Wang C-L., Weng M-I., Liu C-S. Hemoglobin J Meerut: α120 Ala→Glu. Biochim. Biophys. Acta 1974; 351: 7
  • 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
  • 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
  • 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
  • Moo-Penn W. F., Bechtel K. C., Johnson M. H., Jue D. L., Holland S., Huff C., Schmidt R. M. Hemoglobin Jackson, α127 (H10) Lys→Asn. Am. J. Clin. Pathol 1976; 66: 453
  • Kleihauer E. F., Reynolds C. A., Dozy A. M., Wilson J. B., Moores R. R., Berenson M. P., Wright C-S., Huisman T. H.J. Hemoglobin Bibba or α2 136 Pro β2, an unstable α-chaln abnormal hemoglobin. Biochim. Biophys. Acta 1968; 154: 220
  • Clegg J. B., Weatherall D. J., Wong H. B., Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 222: 379
  • Poyart C., Krishnamoorthy R., Bursaux E., Gacon G., Labie D. Structural and functional studies of Haemoglobin Suresnes or α2 141 (HC3) Arg→His β2, a new high oxygen affinity mutant. FEBS Lett. 1976; 69: 103
  • 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
  • Mavilio F., Marinucci M., Tentori L., Fontanarosa P. P., Rossi U., Biagiotti S. Hemoglobin Legnano (α2 141 (HC3) Arg→Leu β2): A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1978; 2: 249
  • 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
  • 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
  • Labossiere A., Vella F., Hiebert J., Galbraith P. Hemoglobin Deer Lodge: α2β2 2 His→Arg. Clin. Biochem. 1972; 5: 46
  • Ingram V. M. Abnormal human haemoglobins. III. The chemical difference between normal and sickle cell haemoglobins. Biochim. Biophys. Acta 1959; 36: 402
  • Hunt J. A., Ingram V. M. Abnormal human haemoglobins. IV. The chemical difference between normal human haemoglobin and Haemoglobin C. Biochim. Biophys. Acta 1960; 42: 409
  • Blackwell R. Q., Oemijati S., Pribadi W., Weng M-I., Liu C-S. Hemoglobin G Makassar: β6 Glu→Ala. Biochim. Biophys. Acta 1970; 214: 396
  • Hill R. L., Swenson R. T., Schwartz H. C. Characterization of a chemical abnormality in Hemoglobin G. J. Biol. Chem. 1960; 235: 3182
  • Tuchinda S., Beale D., Lehmann H. A new haemoglobin in a Thai family. A case of Haemoglobin Siriraj-β-thalassemia. Br. Med. J. 1965; 1: 1583
  • Bonaventura J., Riggs A. Polymerization of hemoglobins of mouse and man. Structural basis. Science 1967; 158: 800
  • Tondo C. V., Bonaventura J., Bonaventura C., Brunori M., Antonini E. Functional properties of Hemoglobin Porto Alegre (α2Aβ2 Ser→Cys) and the reactivity of its extra cysteinyl residue. Biochim. Biophys. Acta 1974; 342: 15
  • 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
  • Monn E., Gaffney P. J., Lehmann H. Haemoglobin Sögn (β14 Arginine). A new haemoglobin variant. Scand. J. Haematol. 1968; 5: 353
  • Beuzard Y., Basset P., Braconnier F., El Gammel H., Martin L., Oudard J. L., Thillet J. Haemoglobin Saki α2β2 14 Leu→Pro (A11) structure and function. Biochim. Biophys. Acta 1975; 393: 182
  • 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 (A11) Leu→Pro). Am. J. Hematol 1976; 1: 283
  • Kennedy C. C., Blundel G., Lorkin P. A., Lang A., Lehmann H. Haemoglobin Belfast β15 (A 12) Tryptophan→Arginine: A new unstable haemoglobin variant. Br. Med. J. 1974; 4: 324
  • Gacon G., Wajeman H., Labie D., Varet B., Christoforov B. A second case of Haemoglobin Belfast (β15 [A 12] Trp→Arg) observed in a French patient. Acta Haematol 1976; 55: 313
  • Baglioni C., Weatherall D. J. Abnormal human hemoglobins. IX. Chemistry of Hemoglobin J Baltimore. Biochim. Biophys. Acta 1963; 78: 637
  • Weatherall D. J. Hemoglobin J (Baltimore) coexisting in a family with Hemoglobin S. Johns Hopkins Hosp. Bull. 1964; 114: 1
  • Chernoff A. I., Perillie P. E. The amino acid composition of HGB New Haven #2 (HGB N New Haven). Biochem. Biophys. Res. Commun. 1964; 16: 368
  • Wong SC, Bouver N., Wilson J. B., Huisman T. H.J. Hb J Georgia = Hb J Baltimore = α2β2 16 Gly→Asp. Clin. Chim. Acta 1971; 35: 521
  • Wade P. T., Jenkins T., Huehns E. R. Haemoglobin variant in a Bushman: Haemoglobin Dβ-Bushmanα2β216Gly→Arg. Nature 1967; 216: 688
  • Maekawa M., Maekawa T., Fujiwara N., Tabara K., Matsuda G. Hemoglobin Nagasaki: αA2β2 17 Glu. A new abnormal human hemoglobin found in one family in Nagasaki. Int. J. Prot. Res. 1970; 11: 147
  • 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
  • Lam H., Wilson J. B., Harris H., Gravely M., Huisman T. H.J. Hemoglobin Alamo [α2β2 19 (B1) Asn→Asp]. Hemoglobin 1977; 1: 703
  • Stamatoyannopoulos G., Nute P. E., Adamson J. W., Bellingham A. J., Funk D., Hornung S. Hemoglobin Olympia (β20 Valine→Methio-nine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J. Clin. Invest. 1973; 52: 342
  • 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
  • Blackwell R. Q., Yang H. J., Wang C. C. Hemoglobin G Taipei: α2β2 22 Glu→Gly. Biochim. Biophys. Acta 1969; 175: 237
  • Vella F., Isaacs W. A., Lehmann H. Hemoglobin G Saskatoon: p22 Glu→AIa. Can. J. Biochem. 1967; 45: 351
  • Blackwell R. Q., Liu C. S., Yang H. J., Wang C. C., Huang J. T.H. Hemoglobin variant common to Chinese and North American Indians: α2β2 22Glu→Ala. Science 1968; 161: 381
  • 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
  • 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→AIa. Am. J. Phys. Anthropol. 1969; 30: 389
  • Rahbar S. Haemoglobin D Iran: β22 Glutamic acid→Glutamine (B4). Br. J. Haematol. 1973; 24: 31
  • Garel M. C., Blouquit Y., Arous N., Rosa J. Hb Strasbourg α2β2 20 (B2) Val→Asp: A variant at the same locus as Hb Olympia β20 Val→Met. FEBS Lett. 1976; 72: 1
  • Forget B. G. Nucleotide sequence of human β globin messenger RNA. Hemoglobin 1977; 1: 879
  • Ranney H. M., Jacobs A. S., Udem L., Zalusky R. Hemoglobin Riverdale-Bronx, an unstable hemoglobin resulting from the substitution of arginine for glycine at helical residue B6 of the β polypeptide chain. Biochim. Biophys. Acta 1968; 33: 1004
  • 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
  • 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
  • Blackwell R. Q., Liu C-S. Hemoglobin G Taiwan-Ami α2β2 25 Gly→Arg. Biochem. Biophys. Res. Commun. 1968; 30: 690
  • Hunt J. A., Ingram V. M. Abnormal human haemoglobins. VI. The chemical difference between Haemoglobins A and E. Biochim. Biophys. Acta 1961; 49: 520
  • Blouquit Y., Arous N., Machado P. E. A., Garel M. C. Hb Henri Mondor: β26 (B8) Glu→Val: A varant with a substitution localized at the same position as that of Hb E β26 Glu→Lys. FEBS Lett. 1976; 72: 5
  • Idelson L. I., Didkowsky 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
  • 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
  • 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 International Congress of Hematology, Sao Paulo, 1972. FEBS Lett. 1973; 33: 37
  • 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
  • Sansone G., Carrell R. W., Lehmann H. Haemoglobin Genova: β28 (BIO) Leucine→Proline. Nature 1967; 214: 877
  • Schmidt R. M., Bechtel K. C., Johnson M. H., Thrrell 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
  • Brimhall B., Jones R. T., Baur E. W., Motulsky A. G. Structural characterization of Hemoglobin Tacoma. Biochemistry 1969; 8: 2125
  • 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
  • Honig G. R., Green D., Shamsuddin M., Vida L. N., Mason R. G., Gnarra D. J., Maurer H. S. Hemoglobin Abraham Lincoln, β32 (B14) Leucine→Proline. An unstable variant producing severe hemolytic disease. J. Clin. Invest. 1973; 52: 1746
  • 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
  • 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
  • Yamaoka K. Hemoglobin Hirose: α2β2 37 (C3) Tryptophan yielding-Serine. Blood 1971; 38: 730
  • Gacon G., Belkhodja O., Wajeman H., Labie D. Structural and functional studies of Hb Rothschild β37 (C3) Trp→Arg. A new variant of the α1β2 contact. FEBS Lett. 1977; 82: 243
  • 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 (β48 (CD6) Leu→Arg). Biochim. Biophys. Acta 1975; 379: 28
  • 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
  • Brown W. J., Niazi G. A., Jayalakshmi M., 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
  • Moo-Penn W. F., Johnson M. H., Bechtel K. C., Jue D. L., Therrell B. L., Schmidt R. M. Hemoglobin Austin and Waco: Two hemoglobins with substitutions in the α1β2 contact region. Arch. Biochem. Biophys. 1977; 179: 86
  • Burkett L. B., Sharma V. S., Pisciotta A. V., Ranney H. M., Bruckheimer S. Hemoglobin Mequon β41 (C7) Phenylalanine→Tyrosine. Blood 1976; 48: 645
  • 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
  • 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
  • Keeling M. M., Ogden L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitchens J. L., Huisman T. H.J. Hemoglobin Louisville (β42 (CD1) Phe→Leu): An unstable variant causing mild hemolytic anemia. J. Clin. Invest. 1971; 50: 2395
  • Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemoglobin Bucuresti β42 (CD1) Phe→Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. Biophys. Acta 1971; 251: 1
  • 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
  • Iuchi I., Ueda S., Hidaka K., Shibata S. Hemoglobin Hoshida (β43 (CD2) Glu→Gln), a new hemoglobin variant discovered in Japan. Hemoglobin 1978; 2: 235
  • 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
  • Sick K., Beale D., Irvine D., Lehmann H., Goodall P. T., Mac-Dougall S. Haemoglobin G Copenhagan and Haemoglobin J Cambridge. Two new β-chain variants of Haemoglobin A. Biochim. Biophys. Acta 1967; 140: 231
  • Marinucci M., Mavilio F., Tentori L., Alberti R. Hemoglobin Gavello α2β247 (CD6) Asp→Gly, a new hemoglobin variant from Polesine (Italy). Hemoglobin 1977; 1: 771
  • Rahbar S., Nowzari G., Ala F. Haemoglobin Avicenna (β47 (CD6) Asp→Ala), a new abnormal haemoglobin. Biochim. Biophys. Acta 1979; 576: 466
  • Charache S., Brimhall B., Milner P., Cobb L. Hemoglobin Okaloosa (β48 (CD7) Leucines→Arginine). An unstable hemoglobin with decreased oxygen affinity. J. Clin. Invest. 1973; 52: 2858
  • Labossiere A., Hill J. R., Vella F. A new βTp V hemoglobin variant: Hb Edmonton. Clin. Biochem. 1971; 4: 114
  • 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
  • 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. Gent. 1971; 8: 302
  • Beresford C. H., Clegg J. B., Weatherall D. J. Haemoglobin Ocho Rios (β52 (D3) Aspartic acid→Alanine); a new β-chain variant of Haemoglobin A found in combination with Haemoglobin S. J. Med. Genet. 1972; 9: 151
  • Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol. 1966; 19: 91
  • Blackwell R. Q., Liu C-S. The identical structural anomalies of Hemoglobins J Meinung and J Korat. Biochem. Biophys. Res. Commun. 1966; 24: 732
  • 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
  • Rahbar S., Nowzari G., Haydari H., Daneshmand P. Haemoglobin Hamadan α2β2 56 Glycine→Arginine (D7). Biochim. Biophys. Acta 1975; 379: 645
  • Giardina B., Brunori M., Antonini E., Tentori L. Properties of Hemoglobin G Ferrara (β57 (E1) Asn→Lys). Biochim. Biophys. Acta 1978; 534: 1
  • 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
  • Boulton F. E., Huntsman R. G., Lehmann H., Lorkin P., Romero Herrera A. Myoglobin variants. Br. J. Haematol. 1971; 20: 671
  • Blackwell R. Q., Liu C-S., Shih T.-B. Hemoglobin J Kaohsiung: β59 Lys→Thr. Biochim. Biophys. Acta 1971; 229: 343
  • Blackwell R. Q., Jim R. T. S., Liu C-S., Weng M-L, Wang C-L., Shih T-B. Fast hemoglobin variant found in Hawaiian-Chinese-Caucasian family in Hawaii and a Chinese subject in Taiwan. Vox. Sang. 1972; 22: 469
  • 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
  • Kagimoto T., Morino Y., Kishimoto S. A new hemoglobin variant Hb Yatsushiro α2Aβ2 60 Val→Leu. Biochim. Biophys. Acta 1978; 532: 195
  • 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
  • Shibata S., Miyaji T., Iuchi I., Ueda S., Takeda I. Hemoglobin Hikari (α2Aβ2 61 Asp→NH2): A fast moving hemoglobin found in two unrelated Japanese families. Clin. Chim. Acta 1964; 10: 101
  • 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
  • Muller C. J., Kingma S. Haemoglobin Zürich α2Aβ2 63 Arg. Biochim. Biophys. Acta 1961; 50: 595
  • Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl. Acad. Sci., USA 1961; 47: 1758
  • 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
  • Murawski K., Szymanowska Z., Kozlowska J. A new variant of abnormal methaemoglobin: Hb M Radom. Biochim. Biophys. Acta 1963; 69: 442
  • Hobolth N. Haemoglobin M Arhus: I. Clinical family study. Acta Paediatr. Scand. 1965; 54: 357
  • 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
  • Betke K., Groschner E., Bock K. Properties of a further variant of Haemoglobin M. Nature 1960; 188: 864
  • Hörlein H., Weber G. Über chronishe familiäre methämoglobinämie und eine neue modifikation des methämoglobins. Deutsche Med. Wschr. 1948; 73: 476
  • 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
  • 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. Z. Kinderheilk. 1975; 120: 69
  • Wajcman H., Krishnamoorthy R., Gacon G., Elion J., Allard C., Labie D. A new hemoglobin variant involving the distal histidine: Hb Bicětre (β63 (E7) His→Pro). J. Mol. Med. 1976; 1: 187
  • Tentori L. Three examples of double heterozygosis beta-thalassemia and rare hemoglobin variants. Intl. Symp. Abnormal Hemoglobin and Thalassemia, IstanbulTurkey, 1974, Abstract 68
  • 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
  • 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
  • Rosa J., Labie D., Wajcman H., Boigne J. M., Cabannes R., Bierme R., Ruffle 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
  • Steadman J. H., Yates A., Huehns E. R. Idiopathic Heinz body anaemia: Hb-Bristol (β67 (E11) Val→Asp). Br. J. Haematol 1970; 18: 435
  • Carrell R. W., Lehmann H., Lorkin P. A., Raik E., Hunter E. Haemoglobin Sydney: β67 (E11) Valine→Alanine: An emerging pattern of unstable haemoglobins. Nature 1967; 215: 626
  • 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
  • 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
  • Kurachi S., Hermodson M., Hornung S., Stamatoyannopoulos G. Structure of Haemoglobin Seattle. Nature New Biol. 1973; 243: 275
  • 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
  • Jones R. T., Brimhall B., Pootrakul S., Gray G. Hemoglobin Vancouver [α2β2 73 (E17) Asp→Tyr]: Its structure and function. J. Mol. Evol 1976; 9: 37
  • Konotey-Ahulu 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
  • Lehmann H., Beale D., Bio-Doku F. S. Haemoglobin GAccra. Nature 1964; 203: 363
  • 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
  • Rieder R. F., Wolf D. J., Clegg J. B., Lee S. L. Rapid postsynthetic destruction of unstable Haemoglobin Bushwick. Nature 1975; 254: 725
  • White J. M., Brain M. C., Lorkin P. A., Lehmann H., Smith M. Mild “unstable haemoglobin haemolytlc anaemia” caused by Haemoglobin Shepherds Bush (β74 (E18) Gly→Asp). Nature 1970; 225: 939
  • 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
  • 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
  • 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). Br. Med. J. 1967; 1: 674
  • Blackwell R. Q., Shih T-B., Wang C-L., Liu C-S. Hemoglobin G-Hsi-Tsou: β79 Asp→Gly. Biochim. Biophys. Acta 1972; 257: 49
  • Benesch R., Edilji R., Benesch R. E. Oxygenation properties of hemoglobin variants with substitutions near the polyphosphate binding site. Biochim. Biophys. Acta 1975; 393: 368
  • Blackwell R. Q., Yang H. T., Wang C. C. Hemoglobin G-Szuhu: β80 Asn→Lys. Biochim. Biophys. Acta 1969; 188: 59
  • Imai K., Morimoto H., Kotani M., Shibata S., Miyaji T., Masutomo K. Studies on the function of abnormal hemoglobins. II. Oxygen equilibrium of abnormal hemoglobins: Shimonaseki, Ube II, Hikari, Gifu, and Agenogi. Biochim. Biophys. Acta 1970; 200: 197
  • Schneider R. G., Hettig R. A., Bilunos M., Brimhall B. Hemoglobin Baylor [α2β2 81 (EF5) Leu→Arg] - an unstable mutant with high oxygen affinity. Hemoglobin 1976; 1: 85
  • 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
  • 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
  • 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
  • Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M. A. F., Nagal K., Lang A., Lehmann H. Hb Helsinki: A variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (β82 [EF6] Lys→Mef). Acta Haematol. 1976; 56: 257
  • Blackwell R. Q., Liu C-S., Wang C-L. Hemoglobin Ta-Li: β83 Gly→Cys. Biochim. Biophys. Acta 1971; 243: 467
  • Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos (α2β2 83 (EF7) Gly→Asp). A new hemoglobin (Hb) variant. Abstract 168. Annual Meeting of the American Society of Hematology, Miami, 1972
  • Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos α2β2 83 (EF7) Gly→Asp: A new hemoglobin variant in double heterozygosity with Hemoglobin S. Blood 1976; 47: 827
  • 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. Abstract 40. Annual Meeting of the American Society of Hematology, Miami, 1972
  • 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
  • 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
  • Hollender A., Lorkin P. A., Lehmann H., Svensson B. New unstable Haemoglobin Borås: β88 (F4) Leucine→Arginine. Nature 1969; 222: 953
  • Opfell R. W., Lorkin P. A., Lehmann H. Hereditary nonspherocytic haemolytlc anaemia with post-splenectomy inclusion bodies and pigmenturia caused by an unstable Haemoglobin Santa Ana — P88 (F4) Leucine→Proline. J. Med. Genet. 1968; 5: 292
  • Thillet J., Blouquit Y., Garel M. C., Dreyfus B., Reyes F., Cohen-Solal M., Beuzard Y., Rosa J. Hemoglobin Creteil B89 (F5) Ser→Asn: High oxygen affinity variant of hemoglobin frozen in a quaternary R-structure. J. Mol. Med. 1976; 1: 135
  • Paniker N. V., Kuang-Tzu Lin Davis, 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
  • 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
  • Schneider R. G., Satoshi U., Alperine 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
  • Ahern E., Ahem C., Hilton T., Serjeant G. R., Serjeant B. E., Seakins M., 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
  • Heller P., Coleman R. D., Yakulis V. Hemoglobin M Hyde Park: A new variant of abnormal methemoglobin. J. Clin. Invest. 1966; 45: 1021
  • Shibata S., Yamamoto K., Ohba Y., Miyaji R., Karita K., Iuchi I. Hemoglobin M Akita disease. Acta Haematol. Jap. 1969; 32: 311
  • Beuzard Y., Courvalin J. CI., 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
  • Aksoy M., Erdem S., Efremov G. D., Wilson J. B., Huisman T. H. J., Schroeder W. A., Shelton J. R., Shelton J. B., Ulitin O. N., Muftuglu A. Hemoglobin Istanbul: Substitution of Glutamine for Histidine in a proximal Histidine (F8(92) β). J. Clin. Invest. 1972; 51: 2380
  • Adams J. G., III, Przywara K. P., Heller P., Shamsuddin M. Hemoglobin J Altgeld Gardens: A hemoglobin variant with a substitution of the proximal histidine of the β-chain. Hemoglobin 1978; 2: 403
  • Finney R., Casey R., Lehmann H., Walker W. Hb Newcastle: P92 (F8) His→Pro. FEBS Lett. 1975; 60: 435
  • 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
  • Gottlieb A. J., Robinson E. A., Itano H. A. Primary structure of Hopkins-I haemoblobin. Nature 1967; 214: 189
  • 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
  • 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
  • Hamilton H. H., Iuchi I., Miyaji T., Shibata S. Hemoglobin 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
  • Moo-Penn W. F., Schneider R. G., Andrian S., Das D. K. Hemoglobin Detroit: β95 (FG2) Lysine→Asparagine. Biochim. Biophys. Acta 1978; 536: 283
  • Lorkin P. A., Lehmann H., Fairbanks V. F., Berglund G., Leonhardt T. Two new pathological haemoglobins: Olmsted β141 (H19) Leu→Arg and Malmö: β97 (FG4) His→Gln. Biochem. J. 1970; 119: 68
  • Taketa F., Huang Y. P., Libnoch J. A., Dessell B. H. Hemoglobin Wood β97 (FG4) His→Leu: A new high-oxygen affinity hemoglobin associ ated with familial erythrocytosis. Biochim. Biophys. Acta 1975; 400: 348
  • Taketa F., Antholine W. E., Mauk A. G., Libnoch J. A. Nitrosyl-hemoglobin Wood: Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum. Biochemistry 1975; 14: 3229
  • Carrell R. W., Lehmann H., Hutchison H. E. Haemoglobin Köln (β98 Valine→Methionine): An unstable protein causing inclusion-body anaemia. Nature 1966; 210: 915
  • Woodson R. D., Heywood J. D., Lenfant C. Oxygen transport in Hemoglobin San Francisco. Clin. Res. 1970; 18: 134
  • Ohba Y., Miyaji T., Shibata S. Identical substitution in Hb Ube-1 and Hb Köln. Nature New Biol. 1973; 243: 205
  • 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. Prod. Roy. Soc. Med. 1973; 66: 507
  • Gacon G., Wajcman H., Labie D. A new unstable hemoglobin mutated in β98 [FG5) Val→Ala: Hb Djelfa. FEBS Lett. 1975; 58: 238
  • Reed C. S., Hampson R., Gordon S., Jones R. T., Novy M. J., Brimhall B., Edwards M. J., Koler R. D. Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, Hemoglobin Kempsey. Blood 1968; 31: 623
  • Jones R. T., Osgood E. E., Brimhall B., Koler R. D. Hemoglobin Yakima: I. Clinical and biochemical studies. J. Clin. Invest. 1967; 46: 1840
  • Weatherall D. J., Clegg J. B., Callender S. T., Wells R. M. G., Gale R. E., Huehns E. R., Perutz M. F., Viggiano G., Ho C. Haemoglobin Radcliffe (α2β2 99 (G1) Ala): A high oxygen-affinity variant causing familial polycythaemia. Br. J. Haematol. 1977; 35: 177
  • Rucknagel D. L., Glynn K. P., Smith J. R. Hemoglobin Ypsilanti characterized by increased oxygen affinity, abnormal polymerization and erythremia. Clin. Res. 1967; 15: 270
  • Lokich J. J., Mahoney C. W., Bunn H. F., Bruckheimer S. M., Ranney H. M. Hemoglobin Brigham (α2Aβ2 100 Pro→Leu). Hemoglobin variant associated with familial erythrocytosis. J. Clin. Invest. 1973; 52: 2060
  • 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
  • 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
  • Mant M. J., Salkie M. L., Cope N., Appling F., Bolch K., Jayalakshmi M., Gravely M., Wilson J. B., Huisman T. H.J. Hb Alberta or α2β2 (101 (G3) Glu→Gly), a new high-oxygen affinity hemoglobin variant causing erythrocytosis. Hemoglobin 1976–77; 1: 183
  • Charache 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
  • 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
  • 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
  • Nagel R. L., Joshua L., Johnson J., Landau L., Bookchin R. M., Harris M. B. Hemoglobin Beth Israel: A mutant causing clinically apparent cyanosis. N. Engl. J. Med. 1976; 295: 125
  • White J. M., Szur L., Gillies I. D. S., Lorkin P. A., Lehmann H. Familial polycythaemia caused by a new haemoglobin variant. Hb Heathrow β103 (G5) Phenylalanine→Leucine. Br. Med. J. 1973; 3: 665
  • Wilkinson T., Chua Ching Geh, Carrell R. W., Robin H., Exner T., Lee Kit Ming, Kronenberg H. A new haemoglobin variant, Haemoglobin Camperdown β104 (G6) Arginine→Serine. Biochim. Biophys. Acta 1975; 393: 195
  • Ryrie D. R., Plowman D., Lehmann H. Haemoglobin Sherwood Forest β104 (G6) Arg→Thr. FEBS Lett. 1977; 83: 260
  • 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; ii: 1170
  • 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
  • Kleihauer E., Waller H. D., Benöhr H. Chr., Kohne E., Gelinsky P. Hb Tübingen. Eine neue β-Kettenvariante (βTp 10–12) mit erhöhter Spontanoxydation. Klin. Wschr. 1971; 48: 651
  • Kohne E., Kley H. P., Kleihauer E., Versmold H., Benohr H. C., Braunitzer G. Structural and functional characteristics of the Hb Tubingen: β106 (G8) Leu→Gln. FEBS Lett. 1976; 64: 443
  • 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. Genet. 1976; 14: 577
  • Imamura T., Fujita S., Ohta Y., Hanada M., Yanese 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
  • 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
  • Nute P. E., Stamatoyannopoulos G., Hermodson M. A., Roth D., Hornung S. Hemoglobinopathic erythrocytosis due to a new electro-phoretically silent variant, Hemoglobin San Diego (β109 (G11) Val→Met). J. Clin. Invest. 1974; 53: 320
  • King M. A. R., Wiltshire B. G., Lehmann H., Morimoto H. An unstable haemoglobin with reduced oxygen affinity: Haemoglobin Peterborough, β111 (G13) Valine→Phenylalanine, its interaction with normal haemoglobin and with Haemoglobin Lepore. Br. J. Haematol. 1972; 22: 125
  • Adams J. G., Boxer L. A., Baehner R. L., Forget B. G., Tsistrokis G. A., Steinberg M. H. Hemoglobin Indianapolis (β112 [G14] Arginine): An unstable β-chain variant producing the phenotype of severe β-thalassemia. J. Clin. Invest. 1979; 63: 931
  • Ranney H. M., Jacobs A. S., Nagel R. L. Haemoglobin New York. Nature 1967; 213: 876
  • Outeirino J., Casey R., White J. M., Lehmann H. Haemoglobin Madrid, β115 (G17) Alanine→Proline: An unstable variant associated with haemolytic anaemia. Acta Haematol. 1974; 52: 53
  • Schneider R. G., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin P (α2β2 117 Arg): Structure and properties. J. Lab. Clin. Med. 1969; 73: 616
  • Schneider R. G., Berkman N. L., Brimhall B., Jones R. T. Hemoglobin Fannin-Lubbock [α2β2 119 (GH2) Gly→Asp]. A slightly unstable mutant. Biochim. Biophys. Acta 1976; 543: 478
  • 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
  • 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 isoelectro-focusing as Hb F. Hemoglobin 1979; 3: 253
  • 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
  • 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
  • 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
  • Baglioni C. Abnormal human haemoglobins. VII. Chemical studies on Haemoglobin D. Biochim. Biophys. Acta 1962; 59: 437
  • Ozsoylo S. Homozygous Hemoglobin D Punjab. Acta Haematol. 1970; 42: 353
  • 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. ScL 1969; 5: 1066
  • Smith E. W., Conley C. L. Sickle cell-Hemoglobin D disease. Ann. Intern. Med. 1959; 50: 94
  • Wasi P., Pootrakul S., Na-Nakorn S., Beale D., Lehmann H. Haemoglobin D Los Angeles (D Punjab, α2β2 125 Glu→NH2) in a Thai family. Acta Haematol 1968; 39: 151
  • Imamura T., Riggs A. Identification of Hemoglobin Oak Ridge with Hemoglobin D Punjab (Los Angeles). Biochem. Genet. 1972; 7: 127
  • Bowman B., Ingram V. M. Abnormal human haemoglobins. VII. The comparison of normal human Haemoglobin D Chicago. Biochim. Biophys. Acta 1961; 53: 569
  • Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229
  • Kamel K., Hoerman K., Awny A. Ethnological significance of hemoglobin α2β2 121 Lys. Am. J. Phys. Anthropol 1970; 26: 107
  • Efremov G. D., Duma H., Rudivic R., Rolovic Z., Wilson J. B., Huis-Man T. H.J. Hemoglobin Beograd or α2β2 121 Glu→Val (GH4). Biochim. Biophys. Acta 1973; 328: 81
  • Clegg J. B., Weatherall D. J., Wong H. B., Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 22: 379
  • Bursaux E., Blouquit Y., Poyart C., Rosa J., Arous N., Bohn B. Hemoglobin Ty Gard (α2Aβ2 124 (H2) Pro→Gln): A stable high O2 affinity variant at the α1β1 contact. FEBS Lett. 1978; 88: 155
  • Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Takenaka H. Japanese haemoglobin variant. Nature 1968; 217: 89
  • Altay C., Altinoz 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
  • 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
  • Blackwell R. Q., Yang Y-J., Wang C-C. Hemoglobin J Taichung: β129 Ala→Asp. Biochim. Biophys. Acta 1969; 194: 1
  • Maniatis A., Bousios T., Nagel R. L., Balazs T., Ueda Y., Bookchin R. M., Maniatis G. M. Hemoglobin Crete (β129 Ala→Pro): A new high-affinity variant interacting with β°- and δp°-thalassemia. Blood 1979; 54: 54
  • 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
  • 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
  • Ohba Y., Miyaji T., 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
  • Brennan S. O., Arnold B., Fleming P., Carrell R. W. A new unstable haemoglobin, β134 Val→Glu. Proc. N.Z. Med. J. 1977; 85: 398
  • Arends T., Lehmann H., Plowman D., Stathopoulou R. Hemoglobin North Shore-Caracas β134 (H12) Valine→Glutamic acid. FEBS Lett. 1977; 80: 261
  • 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
  • Minnich V., Hill R. J., Khuri P. D., Anderson M. E. Hemoglobin Hope: A beta chain variant. Blood 1965; 25: 830
  • Tentori L., Carta Sorcini M., Buccella C. Hemoglobin Abruzzo: Beta 143 (H21) His→Arg. Clin. Chim. Acta 1972; 38: 258
  • 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
  • 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
  • Zak S. J., Brimhall B., Jones R. T., Kaplan M. E. Hemoglobin Andrew-Minneapolis α2Aβ2 144 Lys→Asn: A new high-oxygen affinity mutant human hemoglobin. Blood 1974; 44: 543
  • Hayashi 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
  • 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
  • Charache S., Brimhall B., Jones R. T. Polycythemia produced by Hemoglobin Osier (β145 (HC2) Tyr→Asp). Johns Hopkins Med. J. 1975; 136: 132
  • 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
  • Winslow R. M., Swenberg M-L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin McKees Rocks (α2β2 145 Tyr→Term): A human “nonsense” mutation leading to a shortened β-chain. J. Clin. Invest. 1976; 57: 772
  • Imai K. Oxygen-equilibrium characteristics of abnormal Hemoglobin Hiroshima (α2β2 143 Asp). Arch. Biochem. Biophys. 1968; 127: 543
  • 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
  • Wajcman H., Kilmartin J. V., Najman A., Labie D. Hemoglobin Cochin-Port Royal - consequences of the replacement of the β chain C-terminal by an arginine. Biochim. Biophys. Acta 1975; 400: 354
  • 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
  • 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
  • Ball E. W., Meynell M. J., Beale D., Kynoch P., Lehmann H., Stretton A. O.W. Haemoglobin A2′: α2δ2 16 Glycine→Arginine. Nature 1966; 209: 1217
  • Rieder R. F., Clegg J. B., Weiss H. J., Christy N. P., Rabinowitz R. Hemoglobin A2-Roosevelt: α2δ2 20 Val→Glu. Biochim. Biophys. Acta 1976; 439: 501
  • Jones R. T., Brimhall B., Huisman T. H.J. Structural characterization of two δ chain variants. Hemoglobin A2′ (B2) and Hemoglobin Flatbush. J. Biol. Chem. 1967; 242: 5141
  • Sharma R. S., Harding D. L., Wong S. C., Wilson J. B., Gravely M. E., Huisman T. H.J. A new δ chain variant Haemoglobin A2-Melbourne or α2δ2 43 Glu→Lys (CD2). Biochim. Biophys. Acta 1974; 359: 233
  • Alberti R., Tentori L., Marinucci M., Borghesi V. Hb A2-Adria (δ 51 Pro→Arg (D2)): A new δ-chain variant found in association with β-thalassemia. Hemoglobin 1978; 2: 171
  • 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
  • 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
  • De Jong W. W. W., Bernini L. F. Haemoglobin Babinga (δ136 Glycine→Aspartic acid): A new delta chain variant. Nature 1968; 219: 1360
  • Lie-Injo L. E., Kamuzora H., Lehmann H. Haemoglobin F Malaysia: α2γ2 1 (NA1) Glycine→Cysteine: 136 Glycine. J. Med. Genet. 1974; 11: 25
  • Jenkins G. C., Beale D., Black A. J., Huntsman G. R., Lehmann H. Haemoglobin F Texas I (α2γ2 5 Glu→Lys): A variant of Haemoglobin F. Br. J. Haematol 1967; 13: 252
  • Ahem E. J., Wiltshire B. G., Lehmann H. Further characterization of Haemoglobin F. Texas I γ5 Glutamic acid→Lysine: γ136 Alanine. Biochim. Biophys. Acta 1972; 271: 61
  • Larkin I. L. M., Baker T., Lorkin P. A., Lehmann H., Black A. J., Huntsman R. G. Haemoglobin F Texas II (α2γ2 6 Glu→Lys). The second of the Haemoglobin F Texas variants. Br. J. Haematol. 1968; 14: 233
  • Carrell R. W., Owen M. C., Anderson R., Berry E. Haemoglobin F Auckland G 7 Asp→Asn - further evidence for multiple genes for the gamma chain. Biochim. Biophys. Acta 1974; 365: 323
  • Loukopoulos D., Kaltsoya A., Fessas Ph. On the chemical abnormality of Hb “Alexandra” a fetal hemoglobin variant. Blood 1969; 33: 114
  • Brennan S. O., Smith M. B., Carrell R. W. Haemoglobin F Melbourne Gyl6 Gly→Arg and Haemoglobin F Carlton γ121 Glu→Lys. Biochim. Biophys. Acta 1977; 490: 452
  • Lie-Injo L. E., Wiltshire B. G., Lehmann H. Structural identification of Haemoglobin F Kuala Lumpur (α2γ2 22 (B4) Asp→Gly: (136 Ala). Biochim. Biophys. Acta 1973; 322: 224
  • Ahern E. J., Jones R. T., Brimhall B., Gray R. H. Haemoglobin F Jamaica (α2γ2 61 Lys→Glu: 136 Ala). Br. J. Haematol. 1970; 18: 369
  • Ahern E., Holder W., Ahern V., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin F Victoria Jubilee (α2Aγ2 80 Asp→Tyr). Biochim. Biophys. Acta 1975; 393: 188
  • Schneider R. G., Haggard M. E., Gustavson L. P., Brimhall B., Jones R. T. Genetic haemoglobin abnormalities in about 9000 Black and 7000 White newborns: Haemoglobin F Dickinson (Aγ97His→Arg), a new variant. Br. J. Haematol. 1974; 28: 515
  • 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
  • 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
  • Sacker L. S., Beale D., Black A. J., Huntsman R. G., Lehmann H., Lorkin P. A. Haemoglobin F Hull (γl21 Glutamic acid→Lysine), homologous with Haemoglobins O and O Indonesia. Br. Med. J. 1967; 3: 531
  • Brimhall B., Vedvick T. S., Jones R. T., Ahern E., Palomino E., Ahern V. Haemoglobin F Port Royal (α2Gγ2 125 Glu Ala). Br. J. Haematol. 1973; 27: 313
  • 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: 311
  • Barnabas J., Muller C. J. Haemoglobin Lepore Hollandia. Nature 1962; 194: 931
  • Ostertag W., Smith E. W. Hemoglobin-Lepore Baltimore, a third type of a δβ crossover (δ50, β86). Eur. J. Biochem. 1969; 10: 371
  • 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
  • Ohta Y., Yamaoka K., Sumida I., Yanase T. Hemoglobin Miyada, a β-δ fusion peptide (anti-Lepore) type discovered in a Japanese family. Nature New Biol. 1971; 234: 218
  • Lehmann H., Charlesworth D. Observation on Haemoglobin P (Congo type). Biochem. J. 1970; 119: 43
  • Badr F. M., Lorkin P. A., Lehmann H. Haemoglobin P-Nilotic: containing α β-γ chain. Nature New Biol. 1973; 242: 107
  • 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
  • Milner P. F., Clegg J. B., Weatherall D. J. Haemoglobin H disease due to a unique hemoglobin variant with an elongated α-chain. Lancet 1971; i: 729
  • Weatherall D. J., Clegg J. B. The α-chain-termination mutants and their relation to the α-thalassemias. Phil. Trans. Roy. Soc 1975; B127: 411
  • Clegg J. B., Weatherall D. J., Contopolou-Griva I., Caroutsos K., Poungouras P., Tsevrenis H. Haemoglobin Icaria, a new chain-termination mutant which causes α thalassemia. Nature 1974; 251: 245
  • De Jong 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
  • Flatz G., Kinderlerer J. L., Kilmartin J. V., Lehmann H. Haemoglobin Tak: A variant with additional residues at the end of the β-chains. Lancet 1971; i: 732
  • Imai K., Lehmann H. The oxygen affinity of Haemoglobin Tak, a variant with an elongated β chain. Biochim. Biophys. Acta 1975; 412: 288
  • Lehmann H., Casey R., Lang A., Stathopoulou R., Imai K., Chinda S., Vinai P., Flatz G. Haemoglobin Tak: A β-chain elongation. Br. J. Haematol 1975; 31: 119, (Suppl.)
  • Seid-Akhaven M., Winter W. P., Abramson R. K., Rucknagel D. L. Hemoglobin Wayne: A frameshift mutation detected in human hemoglobin alpha chains. Proc. Natl. Acad. Sci. USA 1976; 73: 882
  • Bunn H. F., Schmidt G. J., Haney D. N., Dluhy R. G. Hemoglobin Cranston, an unstable variant having an elongated β chain due to a nonhomologous crossover between two normal β chain genes. Proc. Natl. Acad. Sci. USA 1975; 72: 3609
  • 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
  • Scott A. F., Phillips J. A., III, Young K. E., Kazazian H. H., Jr., Smith K. D., Charache S., Clegg J. B. The molecular basis of Hemoglobin Grady. Am. J. Hum. Genet. 1981; 33: 129
  • Garel M. C., Goossens M., Oudart J. L., Blouquit Y., Thillet J., Rosa J. Hemoglobin Dakar = Hemoglobin Grady: Demonstration by a new approach to the analysis of the tryptic core region of the a chain and oxygen equilibrium properties. Biochim. Biophys. Acta 1976; 453: 459
  • De Jong W. W. W., Went L. N., Bernini L. F. Haemoglobin Leiden: Deletion of β6 or 7 glutamic acid. Nature 1968; 220: 788
  • Cohen-Solal M., Blouquit Y., Garel M. C., Thillet J., Gaillard L., Creyssel R., Gibaud A., Rosa J. Haemoglobin Lyon (β17–18 (AMIS) Lys-Val→0) determination of sequenator analysis. Biochim. Biophys. Acta 1974; 351: 306
  • Jones R. T., Brimhall B., Huisman T. H. J., Kleihauer E., Betke K. Hemoglobin Freiburg: Abnormal hemoglobin due to deletion of a single amino acid residue. Science 1966; 154: 1024
  • Praxedes H., Lehmann H. Haemoglobin Niteroi - a new unstable variant. Proceedings of the 14th International Congress of Hematology, Sao PauloBrazil, 1972
  • Shibata S., Miyaji T., Ueda S., Matsuoka M., Iuchi I., Yamada K., Shinkai N. Hemoglobin Tochigi (beta 56–59 deleted). A new unstable hemoglobin discovered in a Japanese family. Proc. Jap. Acad. 1970; 46: 440
  • Wajcman H., Labie D., Schapira G. Two new hemoglobin variants with deletion. Hemoglobin Tours: Thr P87 (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
  • 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
  • Lutcher C. L., Huisman T. H.J. Hb-Leslie, an unstable variant due to deletion of Gin β131, occurring in combination with β°-thalassemia, Hb-S, and Hb-C. Clin. Res. 1975; 23: 278A
  • Lutcher C. L., Wilson J. B., Gravely M. E., Stevens P. D., Chen C. J., Linderman J. G., Wong S. C., Miller A., Gottleib M., Huisman T. H.J. Hb Leslie, an unstable hemoglobin due to deletion of glutaminyl residue β131 (H9) occurring in association with β0 -thalassemia, Hb-C, and Hb-S. Blood 1976; 47: 99
  • 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
  • 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→Ala) and Hb Coventry (β141 [H19] Leu→Deleted). Br. J. Haematol. 1978; 38: 195
  • 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
  • Lang A., Lehmann H., McCurdy P. R., Pierce L. Identification of Haemoglobin C Georgetown. Biochim. Biophys. Acta 1972; 278: 57
  • Adams J. G., Heller P. Hemoglobin Arlington Park: A new hemoglobin variant with two amino acid substitutions in the β chain. Hemoglobin 1977; 1: 419
  • Blackwell R. Q., Wong H. B., Liu C-S., Weng M-I. Hemoglobin J Singapore: α78 Asn→Asp: α79 Ala→Gly. Biochim. Biophys. Acta 1972; 278: 482
  • 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
  • Moo-Penn W. F., Schmidt R. M., Jue D. L., Bechtel K. C., Wright J. M., Horne M. K., III, Haycraft C. L., Roth E. F., Nagel R. L. Hemoglobin S Travis. A sickling hemoglobin with two amino acid substitutions [β6 (A3) Glutamic acid→Valine and β142 (H20) Alanine→Valine]. Eur. J. Biochem. 1977; 77: 561
  • Marinucci M., Mavilio F., Massa A., Gabbianelli M., Fontanarosa P. P., Camagna A., Ignesti C., Tentori L. A new abnormal human hemoglobin: Hb Prato (α2 31 (B12) Arg→Ser β2). Biochem. Biophys. Acta 1979; 578: 534
  • Abramov A., Lehmann H., Robb L. Hb Shaare Zedek (β56 E5 Lys→Glu). FEBS Lett. 1980; 113: 235
  • 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→0]. Proc. Natl. Acad. Sci. USA 1981; 78: 469
  • Wajcman H., Elion J., Boissel J. P., Labie D., Jos J., Girot R. A silent hemoglobin variant: Hemoglobin Necker Enfants-Malades (α20 (B1) His→Tyr). Hemoglobin 1980; 4: 177
  • Tatsis B. Hemoglobin Queens (α34 (B15) Leu→Arg): A new variant at the α1β1 contact. Blood 1979; 54: 61a, (Suppl. 1)
  • 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
  • Szelenyi J. G., Horanyi M., Foldi J., Hudacsek J., Istvan L., Hollan S. R. A new hemoglobin variant in Hungary: Hb Savaria - α49(CE7) Ser→Arg. Hemoglobin 1980; 4: 27
  • Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Matsuoka I. Hemoglobin Tottori (α59 [E8] Glycine→Valine) a new unstable hemoglobin. Hemoglobin 1981; 5: 427
  • Spivak V. A., Molchanova T. P., Ermakov N. V., Tokarev Y. N., Martinez G., Szelenyi J., Horanyi M., Foldi J., Hollan S., Kazieva H., Shamov I. A. A new hemoglobin variant: Hb Dagestan α60 (E9) Lys→Glu. Hemoglobin 1981; 5: 133
  • Djoumessi S., Rousseaux J., Descamps J., Goudemand M., Dautrevaux M. Hemoglobin Lille, α2 [74 (EF3) Asp→Ala] β2. Hemoglobin 1981; 5: 475
  • 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
  • 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
  • Shibata S., Ueda S., Miyaji T., Imamura T. Hemoglobinopathies in Japan. Hemoglobin 1981; 5: 509
  • Benesch R. Personal Communication
  • Ohba Y., Miyaji T., Hattori Y., Fuyuno K., Matsuoka M. Unstable hemoglobins in Japan. Hemoglobin 1980; 4: 307
  • 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
  • Schneider R. G., Hightower B., Carpentieri U., Duerst M. L., Shih T. B., Jones R. T. Hemoglobin Oleander α2116 (GH4) Glu→Gln β2]: Structural and functional characterization. Hemoglobin 1980; 6: 465
  • Fleming P. J., Hughes W. G., Farmilo R. K., Wyatt K., Cooper W. N. Hemoglobin Westmead α2122 (H5) His→Gln β2: A new hemoglobin variant with the substitution in the α1β1 contact area. Hemoglobin 1980; 4: 39
  • 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
  • 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. Am. J. Hematol. 1981; 11: 137
  • Shibata S., Miyaji T., Ohba Y. Abnormal hemoglobins in Japan. Hemoglobin 1980; 4: 395
  • Blouquit Y., Braconnier F., Cohen-Solal M., 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
  • 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
  • Marinucci M., Giuliani A., Maffi D., Massa A., Giampaolo A., Mavilio F., Zannotti M., Tentori L. Hemoglobin Bologna (α2β2 61 (E5) Lys→Met) an abnormal human hemoglobin with low oxygen affinity. Biochim. Biophys. Acta 1981; 668: 209
  • Brennan S. O., Wells R. M., Smith H., Carrell R. W. Hemoglobin Brisbane: β68 Leu→His. A new high oxygen affinity variant. Hemoglobin 1981; 5: 325
  • 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
  • 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
  • Blouquit Y., Braconnier F., Galacteros F., Arous N., Soria J., Zittoun R., Rosa J. Hemoglobin Hotel-Dieu β99 Asp→Gly (G1). A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1981; 5: 19
  • 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
  • Moo-Penn W. F., Jue D. L., Johnson M. H., Bechtel K. C., Patchen L. C. Hemoglobin variants and methods used for their characterization during 7 years of screening at the Center for Disease Control. Hemoglobin 1980; 4: 347
  • Moo-Penn W. F., Schneider R. G., Shih T.-B., Jones R. T., Govinda-Rajan S., Govindarajan P. G., Patchen L. C. Hemoglobin Ohio (β142 Ala→Asp): A new abnormal hemoglobin with high oxygen affinity and erythrocytosis. Blood 1980; 56: 246
  • Hirano M., Ohba Y., Imai K., Ino T., Morishita Y., Matsui 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; 57: 697
  • 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. Am. J. Clin. Pathol. 1979; 72: 1028
  • Hayashi A., Fujita T., Fujimura M., Titani K. A new abnormal fetal hemoglobin, Hb F M-Osaka (α2γ2 63 His→Tyr). Hemoglobin 1980; 4: 447
  • 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
  • Adams J. G., III, Morrison W. T., Steinberg M. H. Hemoglobin Parchman: double crossover within a single human gene. Science 1982; 218: 291
  • Honig G. R., Shamsuddin M., Mason R. G., Vida L. N. Hemoglobin Lincoln Park: A δβ fusion (anti-Lepore) variant with an amino acid deletion in the δ chain-derived segment. Proc. Nat. Acad. Sci. USA 1978; 75: 1475
  • Rahbar S., Winkler K., Louis J., Rea C., Blume K., Beutler E. Hemoglobin Great Lakes (β68 [E12] Leucine→Histidine): A new high-affinity hemoglobin. Stood 1981; 58: 813
  • Lee-Potter J. P., Deacon-Smith R. A., Lehmann H., Robb L. Haemoglobin Ferndown (α6 [A4] Aspartic acid→Valine). FEBS Lett. 1981; 126: 117
  • 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
  • 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
  • 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 α1β2 contact. Hemoglobin 1982; 6: 43
  • 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 1982; 6: 379
  • Goossens M., Lee K. Y., Liebhaber S. A., Kan Y. W. Globin structural mutant α125 Leu→Pro is a novel cause of α-thalassaemia. Nature 1982; 296: 864
  • Djoumessi S., Rousseaux J., Dautrevaux M. Structural studies of a new hemoglobin: Hb J Lens, β13 (A10) Ala→Asp. FEBS Lett. 1981; 136: 145
  • Boissel J. P., Wajcman H., Fabritius H., Cabannes R., Labie D. Application of high-performance liquid chromatography to abnormal hemoglobin studies. Characterization of hemoglobin D in Ivory Coast and description of a new variant Hb Cocody (beta 21 (B3) Asp leads to Asn). Biochim. Biophys. Acta 1981; 670: 203
  • Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., Shinohara T., Hori T., Takayama J. Hemoglobin Miyashiro (β23 [B5] Val→Gly) an electrophoretically silent variant discovered by the isopropanol test. Hemoglobin 1981; 5: 653
  • 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
  • Yeager A. M., Zinkham W. H., Jue D. L., Winslow R. M., Johnson M. H., McGuffey J. E., Moo-Penn W. F. Hemoglobin Cheverly: An unstable hemoglobin associated with mild anemia. Pediatr. Res. 1983; 17: 503
  • Spivak V. A., Molchanova T. P., Postnikov Yu. V., Aseeva E. A., Lutsenko I. N., Tokarev Yu. N. A new abnormal hemoglobin: Hb Mozhaisk β92 (F8) His→Arg. Hemoglobin 1982; 6: 169
  • Wajcman H., Aguilar J. L., Bascompte I., Labie D., Poyart C., Bohn B. Structural and functional studies of Hemoglobin Barcelona (α2β2 94 Asp (FGl)→His). J. Mol. Biol. 1982; 156: 185
  • 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
  • Gibb E. A. Increased subunit association of a new superstable variant Hemoglobin Motown. Clin. Res. 1981; 29: 795A
  • Ohta Y., Saito S., Fujita S., Wilson J. B., Lam H., Huisman T. H.J. Hb F-Meinohama or α2β2 (5 Glu→Gly; 75 Ile 136 Gly). Hemoglobin 1981; 5: 565
  • Yoshinaka H., Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K. A new y chain variant, Hb F Kotobuki or AγI 6 (A3) Glu→Gly. Hemoglobin 1982; 6: 37
  • Johnson C. S., Schroeder W. A., Shelton J. B., Shelton J. R. The first example of α deletion in the human a chain: Hemoglobin Boyle Heights or α2 6(A4) Asp→0 β2. Hemoglobin 1983; 7: 125
  • 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
  • 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
  • Webber B. B., Lam H., Wilson J. B., Huisman T. H.J. Hb Albany-GA or α2 11 (A9) Lys→Asn β2. Hemoglobin 1983; 7: 257
  • Honig G. R., Shamsuddin M., Vida L. N., Mompoint M., Bowie L., Jones E., Well S. Hb Evanston (α14 Trp→Arg): A new variant with thalassemia-like hematologic expression. Blood 1982; 60: 53a, (Suppl. 1)
  • 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: 629
  • 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 Lett. 1983; 145: 128
  • Zeng Y-T., Huang S-Z., Zhou X-D., Qui X-K., Dong Q-Y., Li M-Y., Bai J-H. Hb Shenyang [α26 (B7) Ala→Glu]: A new unstable variant found in China. Hemoglobin 1982; 6: 625
  • 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: 53a, (Suppl. 1)
  • Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hemoglobin Tokoname [α139 (HCl) Lys→Thr]: A new hemoglobin variant with a slightly increased oxygen affinity. Hemoglobin 1983; 7: 85
  • Harano T., Harano K., Ueda S., Shibata S., Imai K., Seki M. Hemoglobin Machida [β6 (A31 Glu→Gln], a new abnormal hemoglobin discovered in a Japanese family: structure, function and biosynthesis. Hemoglobin 1982; 6: 531
  • Moo-Perm 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: 91
  • Elion J., Wajcman H., Belkhodja-Dunda O., Lapoumeroulie C., Labie D., Messerschmitt J., Staal A. M., Desableno B. Hemoglobin J Amiens, Beta 17 (A14) Lys replaced by Asn. Coincidence of a functionally silent new abnormal hemoglobin and a polycythemia vera. Nouv. Rev. Fr. d'Hematol 1979; 21: 347
  • 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: 569
  • Arous N., Galacteros F., Fessas Ph., Loukopoulos D., Blouquit Y., Komis G., Sellaye M., Boussiou M., Rosa J. Structural study of Hemoglobin Knossos, β27 (B9) Ala→Ser. A new abnormal hemoglobin present as a silent β-thalassemia. FEBS Lett. 1982; 147: 247
  • 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: 433
  • 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: 413
  • 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 dis-ease. Hemoglobin 1983; 7: 47
  • Lu Y-Q., Fan J-L., Liu J-F., Hu H-L., Peng X-H., Huang P-Y., Chen S-S., Jia P-C, Yang K-G., Liang C-C, Ren X-D., Zuo C-R. Hemoglobin Jianghua [β120 (GH3) Lys→Ile]: A new fast-moving variant found in China. Hemoglobin 1983; 7: 321
  • Kamel K., El-Najjar A., Webber B. B., Chen S. S., Wilson J. B., Kutlar A., Huisman T. H.J. Hb Doha or α2β2 [X-N-Met-1(NAl) Val→Glu]; a new β chain abnormal hemoglobin observed in a Qatari female. Biochim. Biophys. Acta 1985; 831: 257
  • Salkie M. L., Gordon P. A., Rigal W. M., Lam H., Wilson J. B., Headlee M. E., Huisman T. H.J. Hb A2-Canada or α2δ2 99 (G1) Asp→Asn, a newly discovered delta chain variant with increased oxygen affinity occurring in cis to β-thalassemia. Hemoglobin 1982; 6: 223
  • Juricic D., Crepinko I., Efremov G. D., Lam H., Webber B. B., Head-Lee M. G., Huisman T. H.J. Hb A2 Zagreb or α2δ2 125 (H3) Gln→ Glu in association with δβ-thalassemia in a Yugoslavian female. Hemoglobin 1983; 7: 443
  • 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) GIu→Gln: 75 Ile: 136 Ala]. Hemoglobin 1982; 6: 397
  • Nakatsuji T., Headlee M., Lam H., Wilson J. B., Huisman T. H.J. Hb F-Bonaire-Ga or α2Aβ2 39 (C5) Gln→Arg, characterized by high pressure liquid chromatographic and microsequencing procedures. Hemoglobin 1982; 6: 599
  • 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. Biochim. Biophys. Acta 1982; 707: 213
  • Serjeant G. R., Serjeant B. E., Lehmann H., Dukes M., Robb L. Hb F Kingston [Gγ 55 (D6) Met→Arg]. FEBS Lett. 1982; 150: 77
  • Nakatsuji T., Lam H., Huisman T. H.J. Hb F-Kennestone or α2Gγ2 (EF1) 77 His→Arg observed in a Caucasian baby. Hemoglobin 1983; 7: 267
  • Nakatsuji T., Lam H., Carver J., Huisman T. H.J. Hb F-Marietta or Gγ1 80 [EF4] Asp→Asn, observed in a Caucasian baby. Hemoglobin 1982; 6: 407
  • Nakatsuji T., Lam H., Wilson J. B., Webber B. B., Huisman T. H.J. Hb F-Columbus-Ga or α2Gγ2 94 (FG1) Asp→Asn. Hemoglobin 1982; 6: 593
  • Shelton J. B., Shelton J. R., Espinueva Z., Huynh V., Schroeder W. A., Powars D. Hemoglobin F-Caltech: α2Gγ2 120 Lys→Gln. Hemoglobin 1982; 6: 577
  • 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: 79
  • Honig G. R. Personal Communication 1982
  • Bradley T. B. Personal Communication 1982
  • McDonald M. J., Noble R. W., Sharma V. S., Ranney H. M., Crookston J. H., Schwartz J. M. A comparison of the functional properties of two Lepore hemoglobins with those of Hemoglobin A1. J. Mol. Biol. 1975; 94: 305
  • Sugihara J., Imamura T., Kagimoto M., Matsuo T., Yamada H., Imoto T., Yanase T. A new electrophoretic variant of hemoglobin (Munakata) in which a lysine residue is replaced by a methionine residue at position 90 of the α chain. Biochim. Biophys. Acta 1983; 744: 119
  • Ohya Y. Abnormal hemoglobins in North-Kyushu Japan, with special reference to Hb-Kukura and Hb-Fukuoka. Jap. J. Hum. Genet. 1963; 8: 23
  • Moo-Penn W. F., Bechtel K. C., Therrell B. L. Hemoglobin P Nilotic in a Mexican-American family. Hemoglobin 1978; 2: 65
  • Clegg J. B., Weatherall D. J., Milner P. F. Haemoglobin Constant Spring - a chain termination mutant. Nature 1971; 234: 337
  • Strahler J. R., Rosenbloom B. B., Hanash S. M. A silent, neutral substitution detected by reverse-phase high-performance liquid chromatography: Hemoglobin Beirut. Science 1983; 221: 860
  • Harano T., Harano K., Shibata S., Ueda S., Mori H., Arimasa N. Hemoglobin Okayama [β2 (NA2) His→Gln]: a new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3 diphosphoglycerate binding site. FEBS Lett. 1983; 156: 20
  • Wilkinson T., Gough P., Owen M. C., Carrell R. W., Kronenberg H. Detection of variants of haemoglobin D in Australia: Haemoglobin D Camperdown α2β2 121 Glu→Val and Haemoglobin D Punjab2 α2 β2 121 Glu→Gln. Med. J. Aust. 1974; 2: 636
  • Blackwell R. Q., Liu C-S., Wang C-L. Hemoglobin New York in Chinese subjects in Taiwan. Am. J. Phys. Anthropol. 1971; 34: 329
  • Wajcman H., Jones R. T. Proprietes fonctionelles des hemoglobins humaines mutees en position β73. INSERM 1977; 70: 269
  • Shimasaki S., Iuchi I., Hidaka K., Mizuta W. The survey of abnormal hemoglobin in Kobe district. Jap. J. Hum. Genet. 1983; 28: 127
  • Marinucci M., Boissel J. P., Massa A., Wajcman H., Tentori L., Labie D. Hemoglobin Maputo: a new β-chain variant (α2β2 47 (CD6) Asp→Tyr) in combination with Hb S, identified by high performance liquid chromatography (HPLC). Hemoglobin 1983; 7: 423
  • Harano T., Harano K., Shibata S., Ueda S., Imai K., Tsuneshige A., Yamada H., Seki M., Fukui H. Hemoglobin Kariya [α40 (C5) Lys→Glu] a new hemoglobin variant with an increased oxygen affinity. FEBS Lett. 1983; 153: 332
  • Kohne E., Behnken L. J., Leupold D., Rogge H., Martin H., Kleihauer E. Hemoglobin Presbyterian [β108 (G10) Asn→Lys] in a German family. Hemoglobin 1979; 3: 365
  • Como P. F., Barber S., Sage R. E., Trent R. J., Kronenberg H. Hemoglobin Woodville: α6 (A4) Aspartic Acid→Tyrosine. Hemoglobin 1986; 10: 135
  • 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
  • Nakatsuji T., Wilson J. B., Huisman T. H.J. Hb Cordele α2 47 (CE5) Asp→Ala β2 a mildly unstable variant observed in Black twins. Hemoglobin 1984; 8: 37
  • Wong S. C., Ali M. A. M., Pond J. R., Rubin S. M., Johnson S. E. N., Wilson J. B., Huisman T. H.J. Hb J-Singa (α-78 Asn→Asp), a newly discovered hemoglobin variant with the same amino acid substitution as one of the two present in Hb J-Singapore (α-78 Asn→Asp, α-79 Ala→Gly). Biochim. Biophys. Acta 1984; 784: 187
  • Sciarratta G. V., Ivaldi G., Parodi M. I., Sansone G., Molaro G. L., Salkie M. L., Wilson J. B., Reese A. L., Huisman T. H.J. The characterization of Hemoglobin Manitoba or α2 102 (G9) Ser→Arg β and Hemoglobin Contaldo or α2 103 (G10) His→Arg β2 by high performance liquid chromatography. Hemoglobin 1984; 8: 169
  • Cai Y-L., Wang H-B., Yang X-Y., Liu Z-H., Ao Z-F., Gong D-H., Ma J-P., Wang M-J., Ma D-R., Xu Y-Q., Chen E-H. A new fast-moving hemoglobin variant, Hb J Luhe β8 (A5) Lys→Gln. Chinese Hematol. J. 1982; 3: 263
  • Wong S. C., Ali M. A. M., Lam H., Webber B. B., Wilson J. B., Huisman T. H.J. Hemoglobin Hamilton or α2β2 11 (A8) Val→Ile, a silent β-chain variant detected by Triton X-100 acid-urea polyacrylamide gel electrophoresis. Am. J. Hematol. 1984; 16: 47
  • Williamson D., Brennan S. O., Muir H., Carrell R. W. Hemoglobin Collingwood β60 (E4) Val→Ala - a new unstable hemoglobin. Hemoglobin 1983; 7: 511
  • Jen P. C., Chen L. C., Chen P. F., Wong Y., Chen L. F., Guo Y. Y., Chang F. Q., Chow Y. C., Chiu Y. Hemoglobin Quin-Hai, β78 (EF2) Leu→Arg, a new abnor-mal hemoglobin found in Guangdong, China. Hemoglobin 1983; 7: 407
  • Hedlund B., Paine S., Smith C. M., II, Raines J., Morrison W. T., Adams J., III. Hemoglobin Minneapolis-Laos [β-118 (GH1) Phe→Tyr] a new hemoglobin variant with normal functional properties. Hemoglobin 1984; 8: 75
  • Brennan S. O., Williamson D., Smith M. B., Cauchi M. N., Macphee A., Carrell R. W. Hb A2 Victoria δ24 (B6) Gly→Asp, a new δ chain variant occurring with β-thalassemia. Hemoglobin 1984; 8: 163
  • Garcia C. R., Navarro J. L., Lam H., Webber B. B., Headlee M. G., Wilson J. B., Huisman T. H.J. Hb A2-Manzanares or α2δ2 121 (GH4) Glu→Val, an unstable δ chain variant observed in a Spanish family. Hemoglobin 1983; 7: 435
  • Nakatsuji T., Lam H., Huisman T. H.J. Hb F-Calluna or α2γ2 (12 Thr→Arg; 75 Ile; 136 Ala) in a Caucasian baby. Hemoglobin 1983; 7: 563
  • Zeng Y. T., Huang S. Z., Nakatsuji T., Huisman T. H.J. -GγAγ-Thalassemia and γ-chain variants in Chinese newborn babies. Am. J. Hematol 1985; 18: 235
  • Nakatsuji T., Shimizu K., Huisman T. H.J. Hb F-La Grange or α2γ2 101 (G3) Glu→Lys; 75 Ile; 136 Gly; a high oxygen affinity fetal hemoglobin variant observed in a Caucasian newborn. Biochim. Biophys. Acta 1984; 789: 224
  • Blouquit Y., Thillet J., Beuzard Y., Vernant J. P., Dreyfus B. Structural and functional studies of Hemoglobin J Calabria: β64 (E8) Gly→Asp. Biochim. Biophys. Acta 1977; 492: 426
  • Moo-Penn W. F., Baine R. M., Jue D. L., Johnson M. H., McGuffey J. E., Benson J. M. Hemoglobin Evanston: α14 (A12) Trp→Arg, a variant hemoglobin associated with α-thalassemia-2. Biochim. Biophys. Acta 1983; 747: 65
  • Wada Y., Hayashi A., Masanori I., Katakuse T., Ichihara H., Nakabushi T., Matsuo T., Sakurai T., Matsuda H. Characterization of a new fetal hemoglobin variant, Hb F-Izumi Aγ6 Glu→Gly, by molecular secondary ion mass spectrometry. Biochim. Biophys. Acta 1983; 749: 244
  • Rochette J., Poyart C., Varet B., Wajcman H. A new hemoglobin variant altering the α1β2 contact: Hb Chemilly α2β2 99 (G1) Asp→Val. FEBS Lett. 1984; 166: 8
  • Rochette J., Varet B., Boissel J. P., Clough K., Labie D., Wajcman H., Bohn B., Magne P., Poyart C. Structure and function of Hb Saint-Jacques (α2β2 140 (HI8) Ala→Thr): A new high oxygen-affinity variant with altered bisphosphoglycerate binding. Biochim. Biophys. Acta 1984; 785: 14
  • Harano T., Harano K., Shibata S., Ueda S., Mori H., Seki M. Hemoglobin Aichi [α50 (CE8) His→Arg]: A new slightly unstable hemoglobin variant discovered in Japan. FEBS Lett. 1984; 169: 297
  • Chih-Chuan L., Fei X., Kegong Y., Song-Sen C., Peichen J., Maoqi Z., Zhiheng Z. Hemoglobin GuiZhou or α2 77 (EF6) Pro→Argβ2, a new slow-moving hemoglobin variant observed in China. Hemoglobin 1984; 2: 387
  • Zeng Y-T., Huang S-Z., Qiu X-K., Cheng G-C, Ren Z-R., Jin Q-C, Chen C-Y., Jiao C-T., Tang Z-G., Liu R-H., Bao X-H., Zeng L-Z., Duan Y-Q., Zhang G-Y. Hemoglobin Chongqing (α2 (NA2) Leu→Arg) and Hemoglobin Harbin (α16 (A14) Lys→Met) found in China. Hemoglobin 1984; 8: 569
  • Houjun L., Dexiang L., Zhiguo L., Ping L., Ly L., Ji C., Shaozhi H. A new fast-moving hemoglobin variant, Hb J-Tashikuergan α19 (AB1) Ala→Glu. Hemoglobin 1984; 8: 391
  • Jeppsson J. O., Kallman L., Lindgren G., Fagerstam L. G. Hb Linkoping (β36 Pro→Thr): a new hemoglobin mutant characterized by reversed-phase high performance liquid chromatography. J. Chromatogr. 1984; 297: 31
  • Blouquit Y., Delanoe-Garin J., Lacombe C., Arous N., Cayre Y., Peduzzi J., Braconnier F., Galacteros F. Structural study of hemoglobin Hazebrouck, β38 (C4) Thr→Pro: A new abnormal hemoglobin with instability and low oxygen affinity. FEBS Lett. 1984; 172: 155
  • Rahbar S., Asmerom Y., Blume K. G. A silent hemoglobin variant detected by HPLC: Hemoglobin City of Hope β69 (E13) Gly→Ser. Hemoglobin 1984; 8: 333
  • Williamson D., Brennan S. O., Strosberg H., Whitty J., Carell R. W. Hemoglobin A2 Fitzroy δ142 Ala→Asp: A new delta-chain variant. Hemoglobin 1984; 8: 325
  • Moo-Penn W. F., Johnson M. H., McGuffey J. E., Jue D. L. Hemoglobin Shelby [β131 (H9) Gln→Lys]: A correction to the structure of Hemoglobin Deaconess and Hemoglobin Leslie. Hemoglobin 1984; 8: 583
  • Harano K., Harano T., Shibata S., Ueda S., Mori H., Seki M. Hb Okazaki β93 (F8) Cys→Arg], a new hemoglobin variant with increased oxygen affinity and instability. FEBS Lett. 1984; 173: 45
  • Jones R. T., Head C., Shih M. F-C., Shih D. T-B., Dana B., Jones M. B., Koler R. D. Hemoglobin Linkoping [β36 (C2) Pro→Thr] in a large Finnish family from Astoria, Oregon, USA. Hemoglobin 1986; 10: 455
  • Jones R. T., Barwick R. C., Head C. G., Shih F. C., Shih T. B. Hemoglobin Long Island. Abstract 151. 20th Congress of International Society of Haematology, Buenos AiresArgentina, 1984
  • Delanoe-Garin J., Blouquit Y., Arous N., Kister J., Poyart C., North M. L., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Saverne: a new variant with elongated β chains: structural and functional properties. Hemoglobin 1988; 12: 337
  • Wilson C. I. D., Cave R. J., Lehmann H., Close M., Imai K. Haemoglobin Warwickshire (β5 [A2] Pro→Arg): A possible ‘fine tuning’ of 2,3-DPG affinity by β5 Pro. FEBS Lett. 1984; 176: 331
  • Guis M., Mentzer W. C., Jue D. L., Johnson M. H., McGuffey J. E., Moo-Penn W. F. Hemoglobin Twin Peaks α113 (GH1) Leu→His. Hemoglobin 1985; 9: 175
  • Chen S. S., Webber B. B., Wilson J. B., Huisman T. H.J. Hb Gainesville-GA or α2β2 46 (CD5) Gly→Arg. Hemoglobin 1985; 9: 179
  • Delanoe-Garin J., Arous N., Blouquit Y., Hafsia R., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Kenitra α2β2 69 (E13) Gly→-Arg. A new β variant of elevated expression associated with α-thalassemia, found in a Moroccan woman. Hemoglobin 1985; 9: 1
  • Devaraj R., Wilson J. B., Huisman T. H.J. Hb Regina or α2β2 96 (FG3) Leu→Val, a high oxygen affinity variant discovered by cation-exchange HPLC. Am. J. Hematol. 1985; 19: 195
  • Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., Shibata K., Shimokata H., Kuzuya F., Miwa S. A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or β97 (FG4) His→Pro. Hemoglobin 1985; 9: 11
  • Wilson J. B., Webber B. B., Huisman T. H.J. Hb Leslie is the same as Hb Shelby or α2β2 131 (H9) Gln→Lys. Hemoglobin 1984; 8: 595
  • Chen S. S., Wilson J. B., Webber B. B., Huisman T. H. J., Miwa S., Amenomori Y. Hb F-Tokyo or α2Gγ2 34 (B16) Val→Ile, a silent γ chain variant detected by reverse phase high performance liquid chromatography. Hemoglobin 1985; 9: 25
  • Chen S. S., Wilson J. B., Huisman T. H.J. Hb F-Pendergrass, an Aγ1 variant with a Pro→Arg substitution at position γ36 (C2). Hemoglobin 1985; 9: 73
  • Al-Awamy B. H., Niazi G. A., Al-Mouzan M. I., Chen S. S., Wilson J. B., Webber B. B., Huisman T. H.J. Hb F-Damman or α2Aγ2 79 (EF3) Asp→Asn. Hemoglobin 1985; 9: 171
  • Blouquit Y., Lena-Russo D., Delanoe J., Arous N., Bardakdjian J., Lacombe C., Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille α2β2 1 (A1) NH2-Met, 2 (A2) His→3 (A3) Pro: First variant having a N-terminal elongated β chain. Blood 1984; 64: 55a, (Suppl. 1)
  • Shimasaki S. A new hemoglobin variant, Hemoglobin Nunobiki [α141 (HC3) Arg→Cys]. Notable influence of the carboxy-terminal cysteine upon various physico-chemical characteristics of hemoglobin. J. Clin. Invest. 1985; 75: 695
  • Adams J. G., III, Morrison W. T., Pullen D. J., Abney R. L., III, Steinberg M. H. Hemoglobin Mississippi (MS): a new hemoglobin variant with three distinct electrophoretic mobilities. Clin. Res. 1985; 33: 603A
  • Merault G., Keclard L., Saint-Martin C., Jasmin K., Campier A., Delanoe-Garin J., Arous N., Fortune R., Theodore M., Seytor S., Rosa J., Blouquit Y., Galacteros F. Hemoglobin Roseau-Pointe aˇ Pitre α2β2 90 (F6) Glu→Gly: a new hemoglobin variant with slight instability and low oxygen affinity. FEBS Lett. 1985; 184: 10
  • Como P. F., Hocking D., Trent R. J., Kronenberg H. Hb Geelong: β2139 (H17) Asn→Asp. A new hemoglobin with thalassemia-like characteristics. Presented as abstract at February meeting of N.S.W. Thalassemia Society. February, 1985
  • Barwick R. C., Jones R. T., Head C. G., Shih M. F-C., Prchal J. T., Shih D. T-B. Hb Long Island: A hemoglobin variant with a methionyl extension at the NH2 terminus and a prolyl substitution for the normal histidyl residue 2 of the β chain. Proc. Natl. Acad. Sci. USA 1985; 82: 4602
  • Blouquit Y., Arous N., Lena D., Delanoe-Garin J., Lacombe C., Bardakdjian J., Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille [α2β2 N methionyl 2 (NA2) His→Pro]: a new β chain variant having an extended N-terminus. FEBS Lett. 1984; 178: 315
  • Shelton J. B., Shelton J. R., Schroeder W. A., Powars D. R. Hb Aztec or α276 (EF5) Met→Thrβ2 detection of a silent mutant by high performance liquid chromatography. Hemoglobin 1985; 9: 325
  • Harano T., Harano K., Ueda S. Hb Owari [α121 (H4) Val→Met]: a new hemoglobin variant with a neutral-to-neutral amino acid substitution detected by isoelectric focusing. Hemoglobin 1986; 10: 127
  • Bowman J. E., Bloom R., Chen S-S., Webber B. B., Wilson J. B., Kutlar F., Kutlar A., Huisman T. H.J. Hb Chicago or α2 136 (H19) Leu→Met β2. Hemoglobin 1986; 10: 495
  • Rahbar S., Louis J., Lee T., Asmerom Y. Hemoglobin North Chicago (β36 [C2] Proline→Serine): A new high affinity hemoglobin. Hemoglobin 1985; 9: 559
  • Huisman T. H. J., Wilson J. B., Kutlar A., Yang K-G., Chen S-S., Webber B. B., Altay C., Martinez Villegas A. Hb J-Antakya or α2β2 65 (E9) Lys→Met in a Turkish family and Hb Complutense or α2β2 127 (H5) Gln→Glu in a Spanish family; correction of a previously published identification. Biochim. Biophys. Acta 1986; 871: 229
  • Harano T., Harano K., Ueda S., Imai N., Kitazumi T. A new electrophoretically-silent hemoglobin variant: Hemoglobin Kofu or α2β2 84 (EF8) Thr→Ile. Hemoglobin 1986; 10: 417
  • Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K. Hb Himeji or β140 (H18) Ala→Asp, a slightly unstable hemoglobin with increased N-terminal glycation. Hemoglobin 1986; 10: 109
  • Harano K., Harano T., Ueda S., Ohkushi T., Imai K. A new hemoglobin variant, Hb Mito [β144 (HCl) Lys→Glu], with increased oxygen affinity. FEBS Lett. 1985; 192: 75
  • Ohba Y., Igarashi M., Tsukahara M., Nakashima M., Sanada C., Ami M., Arai Y., Miyaji T. Hb A Yokoshima, α2δ225 (B7) Gly→Asp, a new δ chain variant found in a Japanese Family. Hemoglobin 1985; 9: 613
  • Fujita S., Ohta Y., Saito S., Kobayashi Y., Naritomi Y., Kawaguchi T., Imamura T., Wada Y., Hayashi A. Hemoglobin A2 Honai (α2δ290 (F6) Glu→Val): A new delta chain variant. Hemoglobin 1985; 9: 597
  • Hu H., Ma M. Hb F-Urumqi Gγ1 22 (B4) Asp→Gly: a new fetal hemoglobin variant found in a Uygur baby. Hemoglobin 1986; 10: 15
  • Chen S-S., Webber B. B., Kutlar A., Wilson J. B., Huisman T. H.J. Hb F-Cobb or α2Aγ237 (C3) Trp→Gly. Hemoglobin 1985; 9: 617
  • Chen S-S., Wilson J. B., Webber B. B., Huisman T. H.J. Hb F-Beech Island or α2Aγ253 (D4) Ala→Asp. Hemoglobin 1985; 9: 525
  • Boissel J-P., Kasper T. J., Shah S. C., Malone J. I., Bunn H. F. Amino-terminal processing of proteins: Hemoglobin South Florida, a variant with retention of initiator methionine and Nα-acetylation. Proc. Natl. Acad. Sci. USA 1985; 82: 8448
  • Hurt P. J., Fairbanks V. F., Thibodeau S. N., Green M. M., Hoyer J. D., Block S. H., Day C., Jones R. T., Barwick R. C. Hb T-Cambodia, a β chain variant with the mutations of Hb E and Hb D. Punjab, confirmed by DNA analysis. Hemoglobin 1997; 21: 205
  • Moo-Penn W. F., McGuffey J. E., Jue D. L., Johnson M. H., Schum T. Hemoglobin New Mexico: β100 (G2) Pro→Arg. A variant hemoglobin associated with erythrocytosis (BBA 32356). Biochim. Biophys. Acta 1985; 832: 192
  • Lacombe C., Craescu C. T., Blouquit Y., Kister J., Poyart C., Delanoe-Garin J., Arous N., Bardakdjian J., Riou J., Rosa J., Schaeffer C., Galacteros F. Structural and functional studies of hemoglobin Poissy α2β2 56 (D7) Gly→Arg and 86 (F2) Ala→Pro. Eur. J. Biochem. 1985; 153: 655
  • Como P. F., Raven J. L., Wilkinson T., Kronenberg H. Comparison of the six hemoglobin variants occurring at the α6 (A4) position with particular reference to the α6 Asp→Gly substitution found in Perth, Western Australia. Haematology Society of Australia, Perth, Western Australia, October, 1984
  • Chen S. S., Webber B. B., Wilson J. B., Huisman T. H.J. Hb F-Forest Park, a new Aγ variant with two amino acid substitutions, 75(E19)Ile→Thr and 73(E17)Asp→Asn, which can be identified in adults by gene-mapping analysis. Biochim. Biophys. Acta 1985; 832: 242
  • Wada Y., Fujita T., Kidoguchi K., Hayashi A. Fetal hemoglobin variants in 80,000 Japanese neonates: High prevalence of Hb F Yamaguchi (AγT80Asp→Asn). Hum. Genet. 1986; 72: 196
  • Monplaisir N., Merault G., Poyart C., Rhoda M. D., Craescu C. T., Vidaud M., Galacteros F., Blouquit Y., Rosa J. Hb S Antilles (α2β2 6 Glu→Val, 23 Val→Ileu): A new variant with lower solubility than Hb S and producing sickle cell disease in heterozygotes. Proc. Natl. Acad. Sci. USA 1986; 83: 9363
  • Ogata K., Ito T., Okazaki T., Dan K., Nomura T., Nozawa Y., Kajita A. Hemoglobin Sendagi (β42 Phe→Val): a new unstable hemoglobin variant having an amino acid substitution at CD1 of the β-chain. Hemoglobin 1986; 10: 469
  • Baiget M., Gomez Pereira C., Jue D. L., Johnson M. H., McGuffey J. E., Moo-Penn W. F. A case of Hemoglobin Indianapolis [β112 (G14) Cys→Arg] in an individual from Cordoba, Spain. Hemoglobin 1986; 10: 483
  • De Pablos J. M., Wilson J. B., Kutlar A., Chen S. S., Huisman T. H.J. Hb F-Albaicin or Gγ8(AS)Lys→Glu or Gin. Hemoglobin 1986; 10: 655
  • Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Gonzalez Redondo J. M., Huisman T. H.J. Hb F-Clarke or α2Gγ265(E9)Lys→Asn. Hemoglobin 1987; 11: 185
  • Kleman K., Lubin B., Wilson J. B., Kutlar A., Webber B. B., Huisman T. H.J. Hb F-Oakland or α2Gγ1226(B8)Glu→Lys. Hemoglobin 1987; 11: 181
  • Indrak K., Wiedemann B. F., Batek F., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Olomouc or α2β286(F2)Ala→Asp, a new high oxygen affinity variant. Hemoglobin 1987; 11: 151
  • Jen P. C., Liu Y. Hemoglobin Guangzhou, α64(E13)Asp→Gly, a new abnormal hemoglobin found in Guangzhou, China. Hemoglobin 1987; 11: 23
  • Zhou Z-Q., Chen L-C., Chen P-F., Zhang K-Q., Wang Y-H. Hemoglobin Hangzhou, α64(E13)Asp→Gly, a new variant found in China. Hemoglobin 1987; 11: 31
  • Ohba Y., Yamamoto K., Kawata R., Miyaji T. Hyperunstable Hemoglobin Toyama α2136 (H19) Leu→Arg β2 detection and identification by in vitro biosynthesis with radioactive amino acids. Hemoglobin 1987; 11: 539
  • Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., Galacteros F., Feingold J., Rosa J. Hemoglobin La Desirade αA2β2 129 (H7) Ala→Val: A new unstable hemoglobin. Hemoglobin 1986; 10: 593
  • Fleming P. J., Sumner D. R., Wyatt K., Hughes W. G., Melrose W. D., Jupe D. M. D., Baikie M. J. Hemoglobin Hobart or α20(B1) His→Arg: A new α chain hemoglobin variant. Hemoglobin 1987; 11: 211
  • Williamson D., Wells R. M. G., Anderson R., Matthews J. A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [β25(B7)Gly→Asp]. Hemoglobin 1987; 11: 221
  • Masala B., Manca L., Stangoni A., Cuccuru G. B., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Sassari or α2126 (H9)Asp→Hisβ2 observed in a family from Northern Sardinia. Hemoglobin 1987; 11: 373
  • Shih D. T-B., Jones R. T., Shih M. F-C, Jones M. B., Koler R. D., Howard J. Hemoglobin Chico [β66(E10)Lys→Thr]: a new variant with decreased oxygen affinity. Hemoglobin 1987; 11: 453
  • Hu H., Ma M. Hb F-Xinjiang or AγT25(B7)Gly→Arg: a new slow-moving unstable fetal hemoglobin variant. Hemoglobin 1987; 11: 465
  • Ma M., Hu H., Kutlar F., Wilson J. B., Huisman T. H.J. Hb F-Xin-Su or AγT73 (E17) Asp→His: a new slow-moving fetal hemoglobin variant. Hemoglobin 1987; 11: 473
  • Como P. F., Hocking D., Trent R. A., Wilkinson T., Wylie B. R., Bruce D., Kronenberg H. Hb Geelong (β139 Asn→Asp) and Hb Stanmore (β111 Val→AIa). Two new unstable haemoglobins which illustrate the problem of distinguishing a haemoglobin with a thalassaemic phenotype from one inherited along with beta-thalassemia in either cis or trans. Book of Abstracts, XXI Congress of the International Society of Haematology and the XIX Congress of the International Society of Blood Transfusion. 1986, 515
  • Wilkinson T., Como P., Brock P., Kronenberg H., Trent R. J. A., Brennan S. O. Hemoglobin I High Wycombe in an Australian family. Hemoglobin 1987; 11: 51
  • Dahmane-Arbane M., Blouquit Y., Arous N., Bardakdjian J., Benamani M., Riou J., Benabadji M., Rosa J., Galacteros F. Hb Boumerdès α237 (C2)Pro→Argβ2: a new variant in an α chain associated with Hb S in an Algerian family (in French). Nouv. Rev. Fr. d'Hematol. 1987; 29: 317
  • Baklouti F., Giraud Y., Francina A., Richard G., Perier C., Geyssant A., Jaubert J., Brizard C., Delaunay J. Hemoglobin Grange-Blanche [β27(B9) Ala→Val], a new variant with normal expression and increased affinity for oxygen. FEBS Lett. 1987; 223: 59
  • Wada Y., Ikkala E., Imai K., Matsuo T., Matsuda H., Lehtinen M., Hayashi A., Lehmann H. Structure and function of a new hemoglobin variant, Hb Meilahti α2β236(C2)Pro→Thr), characterized by mass spectrometry. Acta Haematol. 1987; 78: 109
  • Zeng Y. T., Ren Z. R., Chen M. J., Zhao J. Q., Qiu X. K., Huang S. Z. A new unstable haemoglobin variant: Hb Shanghai [β131(H9) Gln→Pro] found in China. Br. J. Haematol 1987; 67: 221
  • Gilbert A. T., Fleming P. J., Sumner D. R., Hughes W. G., Ip F., Kwan Y. L., Holland R. A.B. Hemoglobin Randwick or β15(A12) Trp→Gly: A new unstable β-chain hemoglobin variant. Hemoglobin 1988; 12: 149
  • Mrad A., Blouquit Y., Lacombe C., Blibech R., Arous N., Bardakdjian J., Kastally R., Rosa J., Galacteros F. Hb Tunis [α2β2124 (H2) Pro→Ser]. a new β chain variant identified by HPLC. Hemoglobin 1988; 12: 23
  • De Pablos J. M., Kutlar A., Wilson J. B., Webber B. B., Hu H., Huisman T. H.J. Hb D-Granada or α2β222(B4)Glu→Val. Hemoglobin 1987; 11: 563
  • Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J., Delaunay J. Hemoglobin Pierre-Bénite [β90(F6)Glu→Asp], a new high affinity variant found in a French family. Hemoglobin 1988; 12: 171
  • Altay C., Gurgey A., Wilson J. B., Hu H., Webber B. B., Kutlar F., Huisman T. H.J. Hb F-Baskent or α2Aγ128(H6)Ala→Thr. Hemoglobin 1988; 12: 87
  • Malcorra-Azpiazu J. J., Balda-Aguirre M. I., Diaz-Chico J. C., Hu H., Wilson J. B., Webber B. B., Kutlar F., Kutlar A., Huisman T. H.J. Hb Las Palmas or α2β2 49(CD8)Ser→Phe, a mildly unstable hemoglobin variant. Hemoglobin 1988; 12: 163
  • Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., Briere J., Galacteros F. Hemoglobin Brest [β127(H5) Gln→Lys] a new unstable human hemoglobin variant located at the α1β1 interface with specific electrophoretic behavior. Hemoglobin 1988; 12: 179
  • Ali M. A. M., Pinkerton P., Chow S. W. S., Zaetz S. D., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H.J. Some rare hemoglobin variants with altered oxygen affinity; Hb Linkoping [β36(C2)Pro→Thr], Hb Caribbean [β91(F7) Leu→Arg], and Hb Sunny-brook [β36(C2) Pro→Arg]. Hemoglobin 1988; 12: 137
  • Jogessar V. B., Westermeyer K., Webber B. B., Wilson J. B., Hu H., Gonzalez-Redondo J. M., Kutlar A., Huisman T. H.J. Hb Natal or α2(minus Tyr-Arg)β2, a high oxygen affinity a chain variant with a deleted carboxy-terminus resulting from a TAC→TAA (Tyr→terminating codon) mutation in codon α140. Biochim. Biophys. Acta 1988; 951: 36
  • Harano T., Harano K., Imai N., Ueda S., Seki M. An electrophoretically silent hemoglobin variant, Hb Hekinan [α27(B8) Glu→Asp] found in a Japanese. Hemoglobin 1988; 12: 61
  • Malcorra-Azpiazu J. J., Balda-Aguirre M. I., Diaz-Chico J. C., Kutlar F., Kutlar A., Wilson J. B., Hu H., Huisman T. H.J. Hb Le Lamentin or α220(B1)His→Glnβ2 found in a Spanish family. Hemoglobin 1988; 12: 201
  • Wajcman H., Blouquit Y., Gombaud-Saintonge G., Riou J., Galacteros F. Hemoglobin Fontainebleau [α21(B2)Ala→Pro], a new silent mutant hemoglobin. Hemoglobin 1989; 13: 421
  • Wacjman J., Gombaud-Saintonge G., Galacteros F., Martha M., Vertongen F. Hb Belliard [α56(E5)Lys→Asn] a new fast-moving a chain variant found in a subject of Spanish origin. Hemoglobin 1989; 13: 157
  • Gonzalez-Redondo J. M., Wilson J. B., Kutlar A., Huisman T. H. J., Sicilia A., Romero C., Fernandes Fuertes I. Hb J-Pontoise or α263(E12)Ala→Aspβ2 in four members of a Spanish family. Hemoglobin 1987; 11: 47
  • Bardakdjian-Michau J., Lacombe C., Blouquit Y., Craescu C. T., Galacteros F., Lena-Russo D., Orsini A., Vovan L. Hemoglobin N-Timone [α2β28 (A5)Lys→Glu]: A new fast-moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743
  • Gilbert A. T., Fleming P. J., Sumner D. R., Hughes W. G., Holland R. A. B., Tibben E. A. Hemoglobin Windsor or β11(A8)Val→Asp: A new unstable β-chain hemoglobin variant producing a hemolytic anemia. Hemoglobin 1989; 13: 437
  • Gonzalez-Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., Hu H., Wilson J. B., Huisman T. H.J. Hb Monroe or α2β230(B12)Arg→Thr, a variant associated with β-thalassemia due to a G→C substitution adjacent to the donor splice site of the first intron. Hemoglobin 1989; 13: 67
  • Honig G. R., Telfer M. C., Rosenblum B. B., Vida L. N. Hb Warsaw (β42 Phe→Val): An unstable hemoglobin with decreased oxygen affinity. I. Hematologic and clinical expression. Am. J. Hematol. 1989; 32: 36
  • Bernini L. F., Giordano P. C. Hemoglobin Tilburg: α2β273 (E17) Asp→Gly. A new hemoglobin with reduced oxygen affinity. Biochim. Biophys. Acta 1988; 957: 281
  • Hidaka K., Iuchi I., Miyake K., Nakahara H., Iwakawa G. Hb Fukuyama [β77(EF1)His→Tyr]: A new abnormal hemoglobin discovered in a Japanese. Hemoglobin 1988; 12: 391
  • Bardakdjian J., Kister J., Rhoda M. D., Marden M., Arous N., De Leon J., North M. L., Lacombe C., Blouquit Y., Castracane C., Riou J., Rosa J., Galacteros F. Hb J-Cordoba [α2Aβ295(FG2) Lys→Met] a new Hb variant found in Argentina. Hemoglobin 1988; 12: 1
  • Ohba Y., Imai K., Kumada I., Ohsawa A., Miyaji T. Hb Moriguchi or α2β2 97(FG4)Hi→Tyr substitution at the α1-β2 interface. Hemoglobin 1989; 13: 367
  • Kobayashi Y., Fukumaki Y., Komatsu N., Ohba Y., Miyaji T., Miura Y. A novel globin structural mutant, Showa-Yakushiji (β110 Leu-Pro) causing a β-thalassemia phenotype. Blood 1987; 70: 1688
  • Blanke S., Johnsen A., Wimberley P. D., Mortensen H. B. Hemoglobin Hafnia: α2(β116 (G18) His→Gln)2; a new hemoglobin variant mistaken for glycated hemoglobin. Biochim. Biophys. Acta 1988; 955: 214
  • Keclard L., Campier A., Merault G., Auperin A., Riou J., Rosa J., Galacteros F. Hemoglobin Nevers [α2β2130(H8)Tyr→Ser] a new silent variant found in France. Hemoglobin 1990; 14: 103
  • Villegas A., Martin G., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H.J. Hb Extremadura or α2β2133(H11) Val→Leu, a mildly unstable hemoglobin in a Spanish female. Hemoglobin 1989; 13: 505
  • Moo-Penn W. F., Jue D. L., Johnson M. H., Olsen K. W., Shih D., Jones R. T., Lux S. E., Rodgers P., Arnone A. Hemoglobin Brockton [β138(H16) Ala→Pro]: An unstable variant near the C-terminus of the β-subunits with normal oxygen-binding properties. Biochemistry 1988; 27: 7614
  • Moo-Penn W. F., Johnson M. H., Jue D. L., Lonser R. Hemoglobin Hinsdale [β139(H17)Asn→Lys]: A variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate. Hemoglobin 1989; 13: 455
  • De Pablos J. M., Clegg J. B. Hb F-Granada or α2Gγ222(B4)Asp→Val: A new human fetal hemoglobin variant. Hemoglobin 1988; 12: 405
  • Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Hu H., Huisman T. H.J. Hb F-Austell or α2Gγ240(C6)Arg→Lys. Hemoglobin 1988; 12: 409
  • Hidaka K., Iuchi I., Nakahara H., Iwakawa C. Hb F-Fukuyama or AγT43 (CD2)Asp→Asn. Hemoglobin 1989; 13: 93
  • Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H., Orsini A., Rosa J., Galacteros F. Hemoglobin Bruxelles: α2Aβ241 or 42 (C7 or CD1) Phe→deleted. Hemoglobin 1989; 13: 465
  • Moo-Penn W. F., Swan D. C., Hine T. K., Baine R. M., Jue D. L., Benson J. M., Johnson M. H., Virshup D. M., Zinkham W. H. Hb Catonsville (glutamic acid inserted between Pro-37(C2)α and Thr-38(C3)α) - Nonallelic gene conversion in the globin system. J. Biol. Chem. 1989; 264: 21454
  • Kawata R., Ohba Y., Yamamoto K., Miyaji T., Makita R., Ohga K., Watanabe S., Miwa S. Hyperunstable Hemoglobin Koriyama anti-Hb Gun Hill insertion of five residues in the β chain. Hemoglobin 1988; 12: 311
  • Delanoe-Garin J., Blouquit Y., Arous N., Kister J., Poyart C., North M. L., Bardakdjian J., Lacombe C., Rosa J., Galacteros F. Hemoglobin Saverne: A new variant with elongated P chains: Structural and functional properties. Hemoglobin 1988; 12: 337
  • Gale R. E., Blair N. E., Huehns E. R., Clegg J. B. Hb A-like sickle haemoglobin: Hb S-Providence. Br. J. Haematol. 1988; 70: 251
  • Langdown J. V., Williamson D., Knight C. B., Rubenstein D., Carrell R. W. Case Report - A new doubly substituted sickling haemoglobin: HbS-Oman. Br. J. Haematol. 1989; 71: 443
  • Brennan S. O., Williamson D., Symmans W. A., Carrell R. W. Two de novo mutations in one β globin chain: Hemoglobin Atlanta-Coventry, β75 Leu→Pro and β141 Leu→deleted. Hemoglobin 1986; 10: 225
  • Ahmad A., Naqvi S., Ehsanullah S., Zaidi Z. H. Abnormal hemoglobins11 = Hb (Karachi), an α chain abnormality at position 5 Ala→Pro. J. Pakistani Med. Assoc 1986; 36: 206
  • Codrington J. F., Codrington F. A., Wisse J. H., Wilson J. B., Webber B. B., Wong S. C., Huisman T. H.J. Hb Chad or α223(B4) Glu→Lysβ2 observed in members of a Surinam family in association with α-thalassemia-2 and with Hb S. Hemoglobin 1989; 13: 543
  • Bardakdjian-Michau J., Rosa J., Galacteros F., Lancelot M., Marquart F. X. Hb Reims [α223(B4)Glu→Glyβ2]: A new α chain variant with slightly decreased stability. Hemoglobin 1989; 13: 733
  • Groff P., Galacteros F., Kalmes G., Blouquit Y., Wajcman H. Hb Luxembourg [α24(B5)Tyr→His]: A new unstable variant. Hemoglobin 1989; 13: 429
  • Ohba Y., Imai K., Uenaka R., Ami M., Fujisawa K., Itoh K., Hira-Kawa K., Miyaji T. Hb Miyano or α41(C6)Thr→Ser: A new high oxygen affinity α chain variant found in an erythremic blood donor. Hemoglobin 1989; 13: 637
  • Giordano P. C., Fodde R., Amons R., Ploem J. E., Bernini L. F. Hemoglobin J-Anatolia [α61(E10)Lys→Thr]: Structural characterization and gene localization of a new α chain variant. Hemoglobin 1990; 14: 119
  • Wilson J. B., Webber B. B., Kutlar A., Reese A. L., McKie V. C., Lutcher C. L., Felice A. E., Huisman T. H.J. Hb Evans or α262 (E11)Val→MetP2; an unstable hemoglobin causing a mild hemolytic anemia. Hemoglobin 1989; 13: 557
  • Baklouti F., Baudin-Chich V., Kister J., Marden M., Teyssier G., Poyart C., Delaunay J., Wajcman H. Increased oxygen affinity with normal heterotropic effects in hemoglobin Loire [α88(F9) Ala→Ser]. Eur. J. Biochem. 1988; 177: 307
  • Wajcman H., Delaunay J., Francina A., Rosa J., Galacteros F. Hemoglobin Nouakchott [α114(GH2)Pro→Leu]: A new hemoglobin variant displaying an unusual increase in hydrophobicity. Biochim. Biophys. Acta 1989; 998: 25
  • Harkness M., Harkness D. R., Kutlar F., Kutlar A., Wilson J. B., Webber B. B., Codrington J. F., Huisman T. H.J. Hb Sun Prairie or α2130(H13)Ala→Proβ2, a new unstable variant occurring in low quantities. Hemoglobin 1990; 14: 479
  • McDonald M. J., Michalski L. A., Turci S. M., Guillette R. A., Jue D. L., Johnson M. H., Moo-Penn W. F. Structural, functional, and sub-unit assembly properties of Hemoglobin Attleboro [α 138 (H21)Ser→Pro], a variant possessing a site mutation at a critical C-terminal residue. Biochemistry 1990; 29: 173
  • Harano T., Harano K., Ueda S., Imai K., Ohkuma A., Koya Y., Takahashi H. Hb Fukuoka [β2(NA2)His→Tyr]: A new abnormal hemoglobin with a substituted amino acid at the 2,3-diphosphoglycerate binding site. Hemoglobin 1990; 14: 199
  • Yang K. G., Kutlar F., George E., Wilson J. B., Kutlar A., Stoming T. A., Gonzalez-Redondo J. M., Huisman T. H.J. Molecular characterization of β-globin gene mutations in Malay patients with Hb E-β-thalassaemia and thalassaemia major. Br. J. Haematol 1989; 72: 73
  • Vidaud M., Gattoni R., Stevenin J., Vidaud D., Amselem S., Chibani J., Rosa J., Goossens M. A 5′ splice-region G→C mutation in exon 1 of the human β-globin gene inhibits pre-mRNA splicing: A mechanism for β+ -thalassemia. Proc. Natl. Acad. Sci. USA 1989; 86: 1041
  • Li H. J., Zhao X. N., Li H. W., Liang K. X., Wang R. P., Chang T. T., Wilson J. B., Webber B. B., Huisman T. H.J. A new slow-moving hemoglobin variant Hb Tianshui or α2β239(C5)Gln→Arg, observed in a Chinese family living in Gansu. Hemoglobin 1990; 14: 569
  • Honig G. R., Vida L. N., Rosenblum B. B., Perutz M. F., Fermi G. Hemoglobin Warsaw [Pheβ42(CDI)→Val], an unstable variant with decreased oxygen affinity - Characterization of its synthesis, functional properties, and structure. J. Biol. Chem. 1990; 265: 126
  • Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Gainesville-GA or α2β246(CD5)Gly→Arg; second report. Hemoglobin 1989; 13: 623
  • Sciarratta G. V., Ivaldi G. Hb Matera [β55(D6)Met→Lys]: A new unstable hemoglobin variant in an Italian family. Hemoglobin 1990; 14: 79
  • Williamson D., Nutkins J., Rosthoj S., Brennan S. O., Carrell R. W. Characterization of Hb Aalborg, a new unstable hemoglobin variant, by fast atom bombardment mass spectrometry. Hemoglobin 1990; 14: 137
  • Dash S., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Chandigarh or α2β294(FG1)Asp→Gly observed in an Indian family. Hemoglobin 1989; 13: 749
  • Jones R. T., Saointz H. I., Head C., Shih D. T. B., Fairbanks V. F. Hb Johnstown [β109(G11)Val→Leu]: A new electrophoretically silent variant that causes erythrocytosis. Hemoglobin 1990; 14: 147
  • Wajcman H., Mrad A., Blouquit Y., Parmentier C., Riou J., Galacteros F. Hemoglobin Villejuif [β123(H1) Thr→Ile]: A new variant found in coincidence with polycythemia vera. Am. J. Hematol. 1989; 32: 294
  • Harano T., Harano K., Ueda S., Imai K., Marubashi S. Hb Yamagata [β132(H10)Lys→Asn]: A new abnormal hemoglobin in a Japanese family. Hemoglobin 1990; 14: 207
  • Ulukutlu L., Ozsahin H., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H.J. Hb Brockton [α2β2138(H16)Ala→Pro] observed in a Turkish girl. Hemoglobin 1989; 13: 509
  • Martins M. C., Rosado L., Wilson J. B., Kutlar A., Hu H., Huisman T. H.J. Hb Himeji or α2β12140(H18)Ala→Asp in a Portuguese family. Hemoglobin 1989; 13: 411
  • Plaseska D., Li H-J., Wilson J. B., Kutlar F., Kutlar A., Huisman T. H. J., Kulpa J. Hb F-Brooklyn or α2Gγ266 (E10)Lys→Gln. Hemoglobin 1990; 14: 213
  • Priest J. R., Watterson J., Jones R. T., Faassen A. E., Hedlund B. E. Mutant fetal hemoglobin causing cyanosis in a newborn. Pediatrics 1989; 83: 734
  • Glader B. E. Hemoglobin FM-Fort Ripley: Another lesson from the neonate. Pediatrics 1989; 83: 792
  • Plaseska D., Kutlar F., Wilson J. B., Webber B. B., Zeng Y-T., Huisman T. H.J. Hb F-Jiangsu, the first γ chain variant with a valine→methionine substitution: α2Aγ2134(H12)Val→Met. Hemoglobin 1990; 14: 177
  • Harano T., Harano K., Doi K., Ueda S., Imai K., Ohba Y., Kutlar F., Huisman T. H.J. Hb F-Onoda or α2Gγ2146(HC3)His→Tyr, a newly discovered fetal hemoglobin variant in a Japanese newborn. Hemoglobin 1990; 14: 217
  • Codrington J. F., Kutlar F., Harris H. F., Wilson J. B., Stoming T. A., Huisman T. H.J. Hb A2-Wrens or α2δ298 (FG5)Val→Met, an unstable δ chain variant identified by sequence analysis of amplified DNA. Biochim. Biophys. Acta 1989; 1009: 87
  • Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Codrington J. F., Prchal J. T., Hall K. M., De Pablos J. M., Rodriguez I., Huisman T. H.J. Hb Birmingham and Hb Galicia: Two unstable β chain variants characterized by small deletions and insertions. Blood 1990; 75: 1883
  • Ohba Y., Ami M., Imai K., Komatsu K., Amatsu K. Hb Masuda [a114(G16)Leu→Met, 119(GH2)Gly→Asp], a hemoglobin with two substitutions in the β chain. Hemoglobin 1989; 13: 753
  • Wilson J. B., Webber B. B., Plaseska D., De Alarcon P. A., McMillan S. K., Huisman T. H.J. Hb Davenport or α278(EF7)Asn→Hisβ. Hemoglobin 1990; 14: 599
  • Ohba Y., Fujisawa K., Imai K., Leowattana W., Tani Y., Ami M., Miyaji T. A new a chain variant Hb Tonosho [α110(G17) Ala→Thr]: Subunit dissociation during cation exchange chromatography for Hb Alc assay. Hemoglobin 1990; 14: 413
  • Hidaka K., Iuchi I., Kobayashi T., Katoh K., Yaguchi K. Hb Fukutomi [α 126 (H9)Asp→Val]: A new hemoglobin variant with high oxygen affinity. Hemoglobin 1990; 14: 499
  • Plaseska D., Gu L-H., Wilson J. B., Codrington J. F., Huisman T. H. J., Dash S. Hb Sun Prairie or α2130(H13)Ala→Proβ2; second observation in an Indian adult. Hemoglobin 1990; 14: 491
  • Wajcman H., Vasseur C., Blouquit Y., Rosa J., Labie D., Najman A., Reman O., Leporrier M., Galacteros F. Unstable alpha-chain hemoglobin variants with factitius beta-thalassemia biosynthetic ratio: Hb Questembert (α131[H14] Ser→Pro) and Hb Caen (α132 [H15]Val→Gly). Am. J. Hematoi 1993; 42: 367
  • Wajcman H., Blouquit Y., Riou J., Kister J., Poyart C., Soria J., Galacteros F. A new hemoglobin variant found during investigations of diabetes mellitus: Hb Pavie [α135(H18)Val→Glu]. Clin. Chim. Acta 1990; 188: 39
  • Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K. A new hemoglobin variant, Hb Hanamaki or α2139(HCl)Gly→Gluβ2, found in a Japanese family. Hemoglobin 1992; 16: 67
  • Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C., Blouquit Y., Craescu C. T., Galacteros F. Hb N-Timone [α2β28 (A5)Lys→Glu]: A new fast-moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743
  • Spivak V. A. Letter to the Editor. Hemoglobin 1989; 13: 219–220
  • Gaudry C. L., Jr., Pitel P. A., Jue D. L., Hine T. K., Johnson M. H., Moo-Penn W. F. Hb Jacksonville [α2β254(D5)Val→Asp]: A new unstable variant found in a patient with hemolytic anemia. Hemoglobin 1990; 14: 653
  • Podda A., Galanello R., Maccioni L., Melis M. A., Rosatelli C., Perseu L., Cao A. Hemoglobin Cagliari (β60[E4]VaH→Glu): A novel unstable thalassemic hemoglobinopathy. Blood 1991; 77: 371
  • Wajcman H., Kister J., Marden M., Bohn B., Blouqut Y., Descamps J., Goudemand M., Poyart C., Galacteros F. Hemoglobin Calais [β76(E20)Ala→Pro]: A hemoglobin variant with decreased intrinsic oxygen affinity. Biochim. Biophys. Acta 1991; 1096: 60
  • Witkowska H. E., Lubin B. H., Beuzard Y., Baruchel S., Esseltine D. W., Vichinsky E. P., Kleman K. M., Bardakdjian-Michau J., Pinkoski L., Cahn S., Rottman E., Green B. N., Falick A. M., Shackleton C. H.L. Sickle cell disease in a patient with sickle cell trait and compound heterozygosity for Hemoglobin S and Hemoglobin Quebec-Chori. N. Engl. J. Med. 1990; 325: 1150
  • Kutlar F., Felice A. E., Grech J. L., Bannister W. H., Kutlar A., Wilson J. B., Webber B. B., Hu H., Huisman T. H.J. The linkage of Hb Valletta [α2β287(F3)Thr→Pro] and Hb F-Malta-I [α2Gγ2117 G19)His→Arg] in the Maltese population. Hum. Genet. 1991; 86: 591
  • Wajcman H., Vasseur C., Blouquit Y., Esperito Santo D., Peres M. J., Martins M. C., Poyart C., Galacteros F. Hemoglobin Redondo [β92(F8)His→Asn]: An unstable hemoglobin variant associated with heme loss which occurs in two forms. Am. J. Hematol 1991; 38: 194
  • Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M. Hb Isehara (or Hb Redondo) [β92(F8)His→Asn]: An unstable variant with a proximal histidine substitution at the heme contact. Hemoglobin 1991; 15: 279
  • Honig G. R., Vida L. N., Latorraca R., Divgi A. B. Hb South Milwaukee [β105(G7)Leu→Phe]: A newly-identified hemoglobin variant with high oxygen affinity. Am. J. Hematol 1990; 34: 199
  • Harano T., Harano K., Kushida Y., Ueda S. A new abnormal variant, Hb Yahata or β112(G14)Cys→Tyr, found in a Japanese: Structural confirmation by DNA sequencing of the β-globin gene. Hemoglobin 1991; 15: 109
  • Plaseska D., Wilson J. B., Gu L-H., Kutlar F., Huisman T. H. J., Zeng Y-T., Shen M. Hb Zengcheng or α2β2114(G16)Leu→Met. Hemoglobin 1990; 14: 555
  • Plaseska D., De Alarcon P. A., McMillan S., Walbrecht M., Wilson J. B., Huisman T. H.J. Hb Iowa or α2β2119(GH2)Gly→Ala. Hemoglobin 1990; 14: 423
  • Abourzik N. N., Conlon M., Zordon G., Hine T. K., Johnson M. H., Jue D. L., Moo-Penn W. F. Hb St. Francis [β121(GH4)Glu→Gly]: A new mutation at the same site as Hb D-Los Angeles. Hemoglobin 1991; 15: 115
  • Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., Lacombe C., Wini-Chagoon P., Blouquit Y., Riou J., Wasi P., Galacteros F. Hemoglobin Dhonburi α2β2126(H4)Val→Gly: A new unstable β variant producing β-thalassemia intermedia phenotype in association with β0 -thalassemia. Am. J. Hematol. 1990; 35: 96
  • Harano T., Harano K., Kushida Y., Ueda S. Structural analysis of abnormal hemoglobin by the polymerase chain reaction. Jap. J. Clin. Pathol 1990; 38: 1067
  • Plaseska D., Wilson J. B., Kutlar F., Font LI., Baiget M., Huisman T. H.J. Hb F-Catalonia or α2Gγ215(A12)Trp→Arg. Hemoglobin 1990; 14: 511
  • Qualtieri A., Crescibene L., Bagala A., De Marco E. V., Bria M., Brancati C. Hb F-Cosenza or Gγ25(B7)Gly→Glu: A new fast-moving fetal hemoglobin variant. Hemoglobin 1991; 15: 509
  • Huisman T. H. J., Kutlar F., Gu L-H. γ Chain abnormalities and γ-globin gene rearrangements in newborn babies of various populations. Hemoglobin 1991; 15: 393
  • Plaseska D., Kutlar F., Wilson J. B., Fei Y. J., Huisman T. H.J. Hb F-Charlotte, an Aγ variant with a threonine residue in position γ75 and a glycine residue in position γ136. Hemoglobin 1990; 14: 617
  • Harano T., Harano K., Kushida Y., Ueda S., Kawakami H. Hb A2-Niigata [δ1(NAl)VaH→Ala]: A new δ chain variant found in the Japanese population. Hemoglobin 1991; 15: 335
  • Leung H., Gilbert A. T., Fleming P. J., Wong J., Hughes W. G., Hussein S., Nash A. R. Hb A2-Parkville or δ47(CD6)Asp→Val: A new δ chain variant. Hemoglobin 1991; 15: 407
  • Plaseska D., Dimovski A. J., Wilson J. B., Webber B. B., Hume H. A., Huisman T. H.J. Hemoglobin Montreal, a new variant with an extended β chain due to a deletion of Asp, Gly, Leu at positions 73, 74, and 75, and in insertion of Ala, Arg, Cys, Gin at the same location. Blood 1991; 77: 178
  • Vasseur C., Guillemin C., Galacteros F., Wajcman H. Hemoglobin Thionville: An alpha chain variant with substitution of a glutamic residue for valine NA-1 and having an extended N-terminus. Blood 1990; 76: 78a, (Suppl. 1)
  • Lacombe C., Prome D., Blouquit Y., Bardakdjian J., Arous N., Mrad A., Prome J-C., Rosa J. New results of hemoglobin variant structure determinations by fast atom bombardment mass spectrometry. Hemoglobin 1990; 14: 529
  • Wilson J. B., Ramachandran M., Webber B. B., Kutlar F., Hazelwood L. F., Barnett D., Hirschler N. V., Huisman T. H.J. Hb Cleveland or α2β293(F9)Cys→Arg; 121(GH4)Glu→Gln. Hemoglobin 1991; 15: 269
  • Coleman M. B., Steinberg M. H., Adams J. G., III. Hemoglobin Terre Haute arginine β106. A posthumous correction to the original structure of Hemoglobin Indianapolis. J. Biol. Chem. 1991; 266: 5798
  • Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K., Imai K. Hb Kanagawa [α40(C5)Lys→Met]: A new a chain variant with an increased oxygen affinity. Hemoglobin 1992; 16: 1
  • Zwerdling T., Williams S., Nasr S. A., Rucknagel D. L. Hb Port Huron [α56(E5)Lys→Arg]: A new α chain variant. Hemoglobin 1991; 15: 381
  • Perry M. C., Head C., Fairbanks V. F., Jones R. T., Taylor H., Proud V. Hemoglobin Columbia Missouri or α2[88(F9)Ala→Val]β2: A new high-oxygen-affinity hemoglobin that causes erythrocytosis. Mayo Clin. Proc. 1991; 66: 5
  • Langdown J. V., Davidson R. J. L., Williamson D. A new α chain variant, Hb Turriff [α99(G6)Lys→Glu]: The interference of abnormal hemoglobins in Hb Alc determination. Hemoglobin 1992; 16: 11
  • Fujisawa K., Hattori Y., Ohba Y., Ando S. Hb Yuda or α 130 (H13)Ala→Asp: A new α chain variant with low oxygen affinity. Hemoglobin 1992; 16: 435
  • Thein S. L., Best S., Sharpe J., Paul B., Clark D. J., Brown M. J. Hemoglobin Chesterfield (α28 Leu→Arg) produces the phenotype of inclusion body β thalassemia. Blood 1991; 77: 2791
  • Ramachandran M., Gu L-H., Wilson J. B., Kitundu M. N., Adekile A. D., Liu J-C., McKie K. M., Huisman T. H.J. Hb Muscat or α2β232(B14) Leu→Val observed in an Arabian family in association with Hb S. Hemoglobin 1992; 16: 259
  • Molchanova T. P., Wilson J. B., Gu L-H., Guemira F., Fattoum S., Huisman T. H.J. Hb Bab-Saadoun or α2β248(CD7)Leu→Pro, a mildly unstable variant found in an Arabian boy from Tunisia. Hemoglobin 1992; 16: 267
  • Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J. C., Cottenceau D., Galacteros F. Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: The example of Hb La Roche-Sur-Yon [β81(EF5)Leu→His]. Biochim. Biophys. Acta 1992; 1138: 127
  • Tamagnini G. P., Ribeiro M. L., Valente V., Ramachandran M., Wilson J. B., Baysal E., Gu L-H., Huisman T. H.J. Hb Coimbra or α2β299 (Gl)Asp→Glu, a newly discovered high oxygen affinity variant. Hemoglobin 1991; 15: 487
  • Wajcman H., Kister J., Vasseur C., Blouquit Y., Behnken J. L., Galacteros F. Hb Ingelheim [β99(G1)Asp→Glu]: A new high affinity hemoglobin variant destabilizing the α1β2 interrace. Blood 1991; 78: 206a, (Suppl. 1)
  • Como P. F., Wylie B. R., Trent R. J., Bruce D., Volpato F., Wilkinson T., Kronenberg H., Holland R. A. B., Tibben E. A. A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore [β111(G13) Val→Ala]. Hemoglobin 1991; 15: 53
  • Pagano L., Lacerra G., Camardella L., De Angioletti M., Fioretti G., Maglione G., De Bonis C., Guarino E., Viola A., Cutolo R., De Rosa L., Carestia C. Hemoglobin Neapolis, β126(H4)Val→Gly: A novel β-chain variant associated with a mild β-thalassemia phenotype and displaying anomalous stability features. Blood 1991; 78: 3070
  • Duwig I., North M. L., Barth J. G., Rieffel M., Nierengarten P., Arous N., Riou J., Galacteros F. Aspects hematologiques et anomalies structurales d'une nouvelle hemoglobine instable: L'Hb Sarrebourg β131 (H9)Gln→Arg. Ahstract. Nouv. Rev. Fr. d'Hematol. 1987; 29: 344
  • Rahbar S., Lee T., Asmeron Y. Hb Beckman α2β2135(H13)Ala→Glu: A new unstable variant and reduced oxygen affinity. Blood 1991; 78: 204a, (Suppl. 1)
  • Como P. F., Hocking D. R., Swinton G. W., Trent R. J., Holland R. A. B., Tibben E. A., Wilkinson T., Kronenberg H. Hb Geelong [β139(H17)Asn→Asp]. Hemoglobin 1991; 15: 85
  • Moo-Penn W. F., Hine T. K., Johnson M. H., Jue D. L., Holland S., George S., Pierce A. M., Michalski L. A., McDonald M. J. Hb Rancho Mirage [β143(H21)His→Asp]; a variant in the 2,3-DPG binding site showing normal oxygen affinity at physiological pH. Hemoglobin 1992; 16: 35
  • Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., Matsunaga T. Hb Kodaira [β146(HC3)His→Gln]: A new β chain variant with an amino acid substitution at the C-terminus. Hemoglobin 1992; 16: 85
  • Wajcman H., Blouquit Y., Vasseur C., Le Querrec A., Melevendi C., Rasore A., Galacteros F. Two new human hemoglobin variants caused by unusual mutational events: Hb Zaïre contains a five residue repetition within the α-chain and Hb Duino has two residues substituted in the β-chain. Hum. Genet. 1992; 78: 676
  • Trifillis P., Ioannou P., Schwartz E., Surrey S. Identification of four novel δ-globin gene mutations in Greek Cypriots using polymerase chain reaction and automated fluorescence-based DNA sequence analysis. Blood 1991; 78: 3298
  • Abbes S., M'Rad A., Fitzgerald P. A., Dormer P., Blouquit Y., Kister J., Galacteros F., Wajcman H. Hb Al-Ain Abu Dhabi [α18(A16) Gly→Asp]: A new hemoglobin variant discovered in an Emiratee family. Hemoglobin 1992; 16: 355
  • Cürük M. A., Dimovski A. J., Baysal E., Gu L-H., Kutlar F., Molchanova T. P., Webber B. B., Altay C., Gürgey A., Huisman T. H.J. Hb Adana or α259(E8)Gly→Aspβ2, a severely unstable α1-globin variant, observed in combination with the -(α)20.5 kb α-thal-1 deletion in two Turkish patients. Am. J. Hematol. 1993; 44: 270
  • Ferranti P., Palapiano A., Malorni A., Pucci P., Marino G., Cossu G., Manca L., Masala B. Hemoglobin Ozieri: A new α-chain variant [α71(E20)Ala→Val]. Characterization using FAB- and electrospraymass spectrometric techniques. Biochim. Biophys. Acta 1993; 1162: 203
  • Wajcman H., Kister J., Galacteros F., Josifovska O., Spielvolgel A., Nagel R. L. Hb Montefiore [α126(H9)Asp→Tyr]: An abnormal hemoglobin with high oxygen affinity and absence of cooperativity. Blood 1992; 80: 82a, (Suppl. 1)
  • Webber B. B., Wilson J. B., Gu L-H., Huisman T. H.J. Hb Ethiopia or α2140(HC2)Tyr→Hisβ2. Hemoglobin 1992; 16: 441
  • Wajcman H., Kister J., Marden M., Lahary A., Monconduit M., Galacteros F. Hemoglobin Rouen (α-140 (HC2) Tyr→His): alteration of the α-chain C-terminal region and moderate increase in oxygen affinity. Biochim. Biophys. Acta 1992; 1180: 53
  • Liu J-S., Molchanova T. P., Gu L-H., Wilson J. B., Hopmeier P., Schnedl W., Balaun E., Krejs G. J., Huisman T. H.J. Hb Graz or α2β22(NA2)His→Leu; a new β chain variant observed in four families from Southern Austria. Hemoglobin 1992; 16: 493
  • Divoky V., Bisse E., Wilson J. B., Gu L-H., Wieland H., Heinrichs I., Prior J. F., Huisman T. H.J. Heterozygosity for the IVS-I-5 (G→C) mutation with a G→A change at codon 18 (Val→Met; Hb Baden) in cis and a T→G mutation at codon 126 (Val→Gly; Hb Dhonburi) in trans resulting in a thalassemia intermedia. Biochim. Biophys. Acta 1992; 1180: 173
  • Landin B. Hb Karlskoga or α2β221(B3)Asp→His, a new slow-moving variant found in Sweden. Hemoglobin 1993; 17: 201
  • Ward C. M., Fay K. C., Brennan J., Lowrey I., Blacklock H. A. The use of the polymerase chain reaction in the identification of a high oxygen affinity haemoglobin - Hb Finlandia. Aust. New Zeal. J. Med. 1992; 22: 390
  • Molchanova T. P., Postnikov Yu. V., Gu L-H., Prior J. F., Raven J. L., Bennett J. A., Huisman T. H.J. Hb Tigraye or α2β279(EF3)Asp→His(GAC→CAC): A stable hemoglobin variant with increased oxygen affinity observed in an Ethiopian male. Hemoglobin 1993; 17: 247
  • Broxson E. H., Hine T. K., Moo-Penn W. F. Hb Muskegon [β83 (EF7)Gly→Arg]: A new variant found in a family from the U.S. Hemoglobin 1993; 17: 85
  • DeCastro C. M., Lee M., Fleenor D. E., Devlin B., Kaufman R. E. A novel β-globin mutation, βDurham-N.C. [β(114)Leu→Pro], detected by SSCP, produces a dominant thalassemia-like phenotype. Blood 1992; 80: 6a, (Suppl. 1)
  • Welch S., Bateman C. Hb D-Neath or β121(GH4)Glu→Ala: A new member of the Hb D family. Hemoglobin 1993; 17: 255
  • Molchanova T. P., Postnikov Yu. V., Gu L-H., Huisman T. H.J. Hb A2-Grovetown or α2δ275(E19)Leu→Val. Hemoglobin 1993; 17: 289
  • Merritt D., Jones R. T., Head C., Thibodeau S. N., Fairbanks V. F., Steinberg M. H., Coleman M. B., Rodgers G. P. Hb Seal Rock [(α2) 142 Term→Glu, Codon 142 TAA→GAA]: An extended α chain variant associated with anemia, microcytosis, and α-thalassemia-2 (-3.7 kb). Hemoglobin 1997; 21: 331
  • Brennan S. O., Shaw J., Allen J., George P. M. β141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons. Br. J. Haematol. 1992; 81: 99
  • Brennan S. O., Shaw J. G., George P. M., Huisman T. H.J. Post-translational modification of β141 Leu associated with the β75(E19) Leu→Pro mutation in Hb Atlanta. Hemoglobin 1993; 17: 1
  • Hall G. W., Thein S. L., Newland A. C., Chisholm M., Traeger-Synodinos, Higgs D. R. A novel mutation (T-C) in codon 29 of the α2 globin gene produces a structural haemoglobin variant and α thalassaemia. Br. J. Haematol. 1993; 84: 63, (Suppl. 1)
  • Bardakdjian J., Kister J., Wajcman H., Boulard P., Bonn B., Blouquit Y., Galacteros F. Hb Poitiers [α45(CE3)His→Asp]: A new hemoglobin variant with a two-fold increase in oxygen affinity. Hemoglobin 1994; 18: 1
  • Giordano P. C., Harteveld C. L., Streng H., Oosterwijk J. C., Heister J. G. A. M., Amons R., Bernini L. F. Hb Kurdistan [α47(CE5)Asp→Tyr], a new a chain variant in combination with β0 -thalassemia. Hemoglobin 1994; 18: 11
  • Williamson D., Langdown J. V., Myles T., Mason C., Henthorn J. S., Davies S. C. Polycythaemia and microcytosis arising from the combination of a new high oxygen affinity haemoglobin (Hb Luton, α89 His→Leu) and a thalassaemia trait. Br. J. Haematol. 1992; 82: 621
  • Kister J., Soummer A. M., M'rad A., Bohn B., Prome D., Cappellino B., Chambon P., Wajcman H., Galacteros F. Hb Cemenelum [α92 (FG4) Arg→Trp]: A hemoglobin variant with a moderately increased oxygen affinity. Abstract, Journees Scientifiques du Club de L'Hemoglobin, StrasbourgFrance, June, 1993
  • Dincol G., Dincol K., Erdem S., Pobedimskaya D. D., Molchanova T. P., Ye Z., Webber B. B., Wilson J. B., Huisman T. H.J. Hb Capa or α294(G1)Asp→Glyβ2, a mildly unstable variant with an A→G (GAC→GGC) mutation in codon 94 of the α1-globin gene. Hemoglobin 1994; 18: 57
  • Morle F., Francina A., Philippe N., Souillet G., Godet J. Hb Sallanches, a new α chain variant [α2 104(G11)Cys→Tyr] associated with Hb H disease in one homozygous patient. Abstract, Journees Scientifiques du Club de L'Hemoglobine, StrasbourgFrance, June, 1993
  • Wajcman H., Kalmes G., Groff P., Prome D., Riou J., Galacteros F. Hb Melusine [α114(GH2)Pro→Ser]: A new neutral hemoglobin variant. Hemoglobin 1993; 17: 397
  • Wajcman H., Kister J., M'Rad A., Marden M. C., Riou J., Galacteros F. Hb Val de Marne [α133(H16)Ser→Arg]: A new hemoglobin variant with moderate increase in oxygen affinity. Hemoglobin 1993; 17: 407
  • Owen M. C., Hendy J. G. Hb Footscray or α133(H16)Ser→Arg: A new hemoglobin variant. Hemoglobin 1994; 18: 19
  • Langdown J. V., Williamson D., Beresford C. H., Gibb I., Taylor R., Deacon-Smith R. A new β chain variant, Hb Tyne [β5(A2)Pro→Ser]. Hemoglobin 1994; 18: 333
  • Krishnan K., Martinez F., Wille R. T., Jones R. T., Shih D. T., Head C., Fairbanks V. F., Dabich L. Hb Washtenaw [β11(A9)Val→Phe]: An electrophoretically silent, unstable, low oxygen affinity variant associated with anemia and chronic cyanosis. Hemoglobin 1994; 18: 285
  • Pobedimskaya D. D., Molchanova T. P., Amernick R., Druskin M. S., Webber B. B., Wilson J. B., Huisman T. H.J. Hb Sinai-Baltimore or α2β218(A15)Val→Gly, a silent, mildly unstable β chain variant detected by isoelectrofocusing and high performance liquid chromatography. Hemoglobin 1993; 17: 505
  • Coleman M. B., Lu Z-H., Smith C. M., II, Adams J. G., III, Harrell A., Plonczynski M., Steinberg M. H. Two missense mutations in the β-globin gene can cause severe β thalassemia. Hemoglobin Medicine Lake (β32[B14]leucine→glutamine; 98[FG5]valine→methionine. J. Clin. Invest. 1995; 95: 503
  • Owen M. C., Ockelford P. A., Wells R. M.G. Hb Howick [β37 (C3)Trp→Gly]: A new high oxygen affinity variant of the α1β1 contact. Hemoglobin 1993; 17: 513
  • Stabler S., Jones R. T., Head C., Shih D. T. B., Fairbanks V. F. Hemoglobin Denver, beta 41(C7) Phe→Ser: A low O2 affinity Hb variant associated with chronic cyanosis and hemolysis. Blood 1993; 82: 222a, (Suppl. 1)
  • Molchanova T. P., Postnikov Yu. V., Pobedimskaya D. D., Smetanina N. S., Moschan A. A., Kazanetz E. G., Tokarev Yu. N., Huisman T. H.J. Hb Alesha or α2β267(E11)Val→Met: A new unstable hemoglobin variant identified through sequencing of amplified DNA. Hemoglobin 1993; 17: 217
  • Fay K. C., Brennan S. O., Costello J. M., Potter H. C., Williamson D. A., Trent R. J., Ockelford P. A., Boswell D. R. Haemoglobin Manukau β67(E11)Val→Gly: Transfusion-dependent haemolytic anaemia ameliorated by coexisting alpha thalassaemia. Br. J. Haematol. 1993; 85: 352
  • Wajcman H., Kister J., Prome D., Galacteros F., Gilsanz F. Hb Villaverde [β89(F5)Ser→Arg]: The structural modification of an intra-subunit contact is responsible for a high oxygen affinity. Biochim. Biophys. Acta 1994; 1225: 89
  • Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T. P., Huisman T. H.J. Hb Hradec Kralove (Hb HK) or α2β2115(G17)Ala→Asp, a severely unstable hemoglobin variant resulting in a dominant β-thalassemia trait in a Czech family. Hemoglobin 1993; 17: 319
  • Girodon E., Ghanem N., Vidaud M., Riou J., Martin J., Galacteros F., Goossens M. Rapid molecular characterization of mutations leading to unstable hemoglobin β-chain variants. Ann. Hematol 1992; 65: 188
  • Wajcman H., Girodon E., Promé D., North M. L., Plassa F., Duwig I., Kister J., Bergerat J. P., Oberling F., Lampert E., Lonsdorfer J., Goossens M., Galacteros F. Germline mosaicism for an alanine to valine substitution at residue β140 in hemoglobin Puttelange, a new variant with high oxygen affinity. Hum. Genet. 1995; 96: 711
  • Pobedimskaya D. D., Molchanova T. P., Huisman T. H. J., Harding S. R., Bakanec R. Hb F-Saskatoon or α2Gγ221(B3)Glu→Lys observed in a North American Indian newborn. Hemoglobin 1993; 17: 547
  • Pobedimskaya D. D., Molchanova T. P., Gu L-H., Molina M. A., De Pablos J. M., Huisman T. H.J. Hb F-Sacromonte or α2Gγ259(E3) Lys→Gln observed in a Spanish new-born and his mother. Hemoglobin 1993; 17: 269
  • Ferranti P., Barone F., Pucci P., Malorni A., Marino G., Pilo G., Manca L., Masala B. Hb F-Sassari: A novel Gγ variant with a threonine residue at position γ75, characterized by mass spectrometric techniques. Hemoglobin 1994; 18: 307
  • Qin W-B., Ju T-L., Yue X-L., Yan X-L., Qin L-Y., Molchanova T. P., Pobedimskaya D. D., Huisman T. H.J. Hb A2-Liangcheng [δ117 (G19)Asn→Asp(AAC→GAC)]: A new δ chain variant detected by gene analysis in a Chinese family. Hemoglobin 1993; 17: 463
  • Galacteros F., Girodon E., M'Rad A., Martin J., Goossens M., Jaber L., Cohen I. J., Tamary H., Goshen Y., Zaizov R., Wajcman H. Hb Taybe (α38 or 39 THR deleted): an α-globin defect, silent in the heterozygous state and producing severe hemolytic anemia in the homozygous. C.R. Acad. Sci. 1994; 317: 437
  • Fujisawa K., Yamashiro Y., Hattori Y., Ohba Y., Kajita T., Kageyama S., Arita J. Hb Higashitochigi (Hb HT) [β24(B6) or β25(B7) glycine deleted]: A new unstable variant expressing cyanosis. Hemoglobin 1993; 17: 467
  • Pobedimskaya D. D., Molchanova T. P., Streichman S., Huisman T. H.J. Compound heterozygosity for two α-globin gene defects, Hb Taybe (α1; 38 or 39 minus Thr) and a poly A mutation (α2; AATAAA→AATAAG), results in a severe hemolytic anemia. Am. J. Hematol. 1994; 47: 198
  • Wajcman H., Bost M., Blouquit Y., Préhu C., Riou J., Galacteros F. Two new α chain variants found during glycated hemoglobin screening: Hb Tatras [α7(A5)Lys→Asn] and Hb Lisbon [α23(B4)Glu→Asp]. Hemoglobin 1994; 18: 427
  • Harano T., Harano K., Imai K., Murakami T., Matsubara H. Hb Kurosaki [α7(A5)Lys→ Glu]: A new α chain variant found in a Japanese woman. Hemoglobin 1995; 19: 197
  • Pobedimskaya D. D., Molchanova T. P., Huisman T. H.J. Hb Ramona or α224(B5)Tyr→Cysβ2. Hemoglobin 1994; 18: 365
  • Wajcman H., De Montalembert M., Girot R., Kister J., Maier-Redelsperger M., Galacteros F. The use of staphylococcus V8 protease in the structural determination of human hemoglobin variants: Hb Valparaiso [α88(F9)Ala→Gly] as example. Hemoglobin 1994; 18: 275
  • Kister J., Kiger L., Francina A., Hanny P., Szymanowicz A., Blouquit Y., Prome D., Galactéros F., Delaunay J., Wajcman H. Hb Roanne [α94(Gl)Asp→Glu]: A variant of the α1β2 interface with an unexpected high oxygen affinity. Biochim. Biophys. Acta 1995; 1246: 34
  • Kazanetz E. G., Leonova Ye. J., Wilson J. B., McMillan S. K., Walbrecht M., De Pablos Gallego J. M., Huisman T. H.J. Hb Anamosa or α2111(G18)Ala→Va1β2 (α2 mutation) and Hb Mulhacen or α2l23(H6) Ala→Serβ2 (α1 mutation) are two silent, stable variants detected by sequencing of amplified DNA. Hemoglobin 1995; 19: 1
  • Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris Ph. Haemoglobin Tuniz-Bizerte: a new α1 globin 129 Leu→Pro unstable variant with thalassaemic phenotype. Br. J. Haematol. 1995; 90: 71
  • Landin B., Berglund S., Lindoff B. Hb Trollhättan [β20(B2)Val→Glu] - a new haemoglobin variant with increased oxygen affinity causing erythrocytosis. Eur. J. Haematol. 1994; 53: 21
  • Gürgey A., Altay C., Gu L-H., Leonova Ye. J., Delibalta A., Öner C., Huisman T. H.J. Hb Hakkari or α2β231(B13)Leu→Arg, a severely unstable hemoglobin variant associated with numerous intraerythroblastic inclusions and erythroid hyperplasia of the bone marrow. Hemoglobin 1996; 19: 165
  • Vassilopoulos G., Papassotiriou I., Voskaridou E., Stamoulakatou A., Premetis E., Kister J., Marden M., Griffon N., Poyart C., Wajcman H., Galactéros, Loukopoulos D. Hb Arta [β45 (CD4) Phe→Cys]: a new unstable haemoglobin with reduced oxygen affinity in trans with β-thalassaemia. Br. J. Haematol. 1995; 91: 595
  • Rochette J., Barnetson R., Kiger L., Kister J., Littlewood T. J., Webster R., Poyart C., Thein S. L. Association of a novel high oxygen affinity haemoglobin variant with δβ thalassaemia. Br. J. Haematol. 1994; 86: 118
  • Harano T., Harano K., Katuki T. Hb Yaizu [β79(EF3)Asp→Asn]: A new β chain variant found in a Japanese female. Hemoglobin 1995; 19: 21
  • Wajcman H., Behnken L. J., Riou J., Galacteros F. Hb Mainz [β98(FG5)Val→Glu]: A new unstable variant carrying a structural modification at the same position as Hb Koln. Abstract 258. Br. J. Haematol. 1994; 87, (Suppl. 1)
  • Wajcman H., Kister J., M'Rad A., Promé D., Milpied N., Rapp M. J., Harousseau J. L., Riou J., Bardakdjian J., Galacteros F. Hb Saint Nazaire (β103[G5]Phe→Ile): A new example of polycythemia due to a hemoglobin variant with increased oxygen affinity. Am. J. Hematol. 1993; 44: 16
  • Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J. S. Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [β139 (H17)Asn→Tyr]. Hemoglobin 1995; 19: 335
  • Abbes S., Fitzgerald P. A., Varady E., Girot R., Pic P., Blouquit Y., Ducrocq R., Drupt F., Wajcman H. Two fetal hemoglobin variants affecting the same residue: Hb F-Emirates [Gγ59(E3)[Lys→Gln] and Hb F-Foch [Gγ59(E3)Lys→Gln]. Hemoglobin 1995; 19: 173
  • Plaseska D., Panovska-Popovska S., Lazervski M., Efremov G. D. Hb F-Macedonia-II [Gγ104(G6)Lys→Asn]: A new γ chain variant. Hemoglobin 1994; 18: 373
  • Plaseska D., Cepreganova-Krstik B., Momirovska A., Efremov G. D. Hb F-Macedonia-I or α2Aγ22(NA2)His→Gln. Hemoglobin 1994; 18: 241
  • Loudianos G., Porcu S., Cossu P., Tannoia N., Vitucci A., Campanale D., Cao A., Pirastu M. A new δ-chain variant Hemoglobin A2-Puglia or α2δ2 26 Glu→Asp (B8), detected by DNA analysis in a family of Southern Italian origin. Hum. Mut. 1993; 2: 327
  • Galanello R., Gasperini D., Perseu L., Barella S., Ideo A., Cao A. Hb A2-Sant Antioco [α2δ293(F9)Cys→Gly]: A new δ chain variant identified by sequencing of amplified DNA. Hemoglobin 1994; 18: 437
  • Préhu M-O., Préhu C., Goossens M., Galactéros F., Wajcman H. A new anti-Lepore hemoglobin, Hb P India (β87-δ105), found in coincidence with a C→G substitution at position 162 of IVS-2 in both the δ and βδ genes, questions on the genetic mechanisms leading to Hbs Lepore and anti-Lepore. Blood 1994; 83: 261a, (Suppl. 1)
  • Waye J. S., Eng B., Patterson M., Chui D. H. K., Olivieri N. F. Identification of a novel termination codon mutation (TAAβTAT, Term→Tyr) in the α2 globin gene in a Laotian girl with Hemoglobin H disease. Blood 1994; 83: 3418
  • Wajcman H., Kister J., Promé D., Blouquit Y., Préhu C., Poyart C., Galactéros F. Interaction of 2 amino acid substitutions within the same β chain of human hemoglobin: the examples of Hb Corbeil and Hb Villeparisis. C.R. Acad. Sci. 1995; 318: 785
  • Wajcman H., Blouquit Y., Laharry A., Soummer A. M., Groff P., Bardakdjian J., Préhu C., Riou J., Godard C., Galactèros F. Three new neutral α chain variants: Hb Bois Guillaume [α65(E14)Ala→Val], Hb Mantes-La-Jolie [α79(EF8)Ala→Thr], and Hb Mosella [α111(G18)Ala→Thr]. Hemoglobin 1995; 19: 281
  • Giordano P. C., Harteveld C. L., Kok P. J. M. J., Geenen A., Batelaan D., Amons R., Bernini L. F. Hb Gouda [α72(EFl)His→Gln], a new silent α chain variant. Hemoglobin 1996; 20: 21
  • Harano T., Harano K., Uehara S., Matsushita K. Two new a chain variants: Hb Fuchu-I [α72(EF1)His→Tyr] and Hb Fuchu-II [α97(G4)Asn→His]. Hemoglobin 1995; 19: 389
  • Wajeman H., Promé D., Riou J., Mathis M., Godart C., Hurtrel D., Préhu C., Bardakkjian J., Bridey F., Galactéros F. Hb Saclay [α133(H16)Ser→Asn]: a new neutral variant. Abstract 48. Nouv. Rev. Fr. d'Hematol 1996; 38: 27
  • Harano K., Harano T., Koide G., Akimaru S. Hb Nakano [β8 (Lys→Met]: a new β chain variant found in a Japanese woman. Hemoglobin 1995; 19: 397
  • Beris Ph., Darbellay R., Frutiger A., Hochstrasser D. Hb Iraq-Halabja 10(a7) Ala→Val (GCC→GIC): a new β-chain variant that produces no significant clinical or hematological alterations. Blood 1995; 86: 642a, (Suppl. 1)
  • Wajcman H., Promé D., Kister J., Davies S. C., Galactéros F., Henthorn J. S. Hb Uxbridge [β20(B2)Val→Gly]: a new hemoglobin variant with mild increase in oxygen affinity found on neonatal screening. Hemoglobin 1996; 20: 339
  • Lacan P., Francina A., Promé C., Galactéros F., Wajcman H. Hb Aubenas [β26(B8)Glu→Gly]: a new variant normally synthesized affecting the same codon as in Hb E. Hemoglobin 1996; 20: 113
  • Seelig H. P. Hb Karlsruhe [β28(B10)Leu→Met]: a new unstable β-globin mutant causing cyanosis and methemoglobinemia. Personal communication 1995
  • Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M. C., Cao A., Breitenstein U., Fehr J., Tuchschmid P. Hb Hinwil or β38(C4)Thr→Asn: a new β chain variant detected in a Swiss family. Hemoglobin 1996; 20: 31
  • Kiger L., Groff P., Kalmes G., Kister J., Promé D., Galactéros F., Wajcman H. Hb J-Europa [β62(E6)Ala→Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin 1996; 20: 135
  • Rodriguez Romero W. E., Castillo M., Chaves M. A., Saenz G. F., Gu L-H., Wilson J. B., Baysal E., Smetanina N. S., Leonova J. Y., Huisman T. H.J. Hb Costa Rica or α2β277(EF1)His→Arg; the first example of a somatic cell mutation in a globin gene. Hum. Genet. 1996; 97: 829
  • Ohba Y., Yamada H., Takamatsu S., Imai K. Hb Tsurumai [β82 (EF6)Lys→Gln]: a new Hb variant with high oxygen affinity and eryfhrocytosis. Hemoglobin 1996; 20: 141
  • Lacan P., Kister J., Francina A., Souillet G., Galactéros F., Delaunay J., Wajcman H. Hemoglobin Debrousse (β96[FG3] Leu→Pro): a new unstable hemoglobin with twofold increased oxygen affinity. Am. J. Hematol 1996; 51: 276
  • Kister J., Papassotiriou I., Groff P., Kalmes G., Promé D., Wajcman H. Structural and functional characterisation of a new electrophoretically silent hemoglobin variant. Ahstract 46. Nouv. Rev. Fr. d'Hematol 1996; 38: 26
  • Gray G. R., Manson H. E., Gu L-H., Leonova J. Ye., Huisman T. H.J. Hb Lulu Island (α2β2107[G9]Gly→Asp)-β0-thalassemia (codon 15; TGG→TAG), a form of thalassemia intermedia. Am. J. Hematol. 1995; 50: 26
  • Harano T., Harano K., Kawasaki R., Kawakami K. Hb Toranomon [β112(G14)Cys→Trp]: a new unstable and electrophoretically silent hemoglobin variant. Hemoglobin 1996; 20: 361
  • Hutt P. J., Fairbanks V. F., Griffin T. C., Thibodeau S. N., Green M. M., Hoyer J. D. Hb Cook [β132(H10)Lys→Thr]: a new hemoglobin variant in a Southeast Asian family. Hemoglobin 1996; 20: 371
  • Fairbanks V., McCormick D., Horn A., Jones R., Shih D., Hoyer J., Madden B. J., Kubik K. Hemoglobin Old Dominion, β143 (H21) His→Tyr: a new variant causing spurious elevation of Hb Alc. Blood 1995; 86: 647a, (Suppl. 1)
  • De Pablos Gallego J. M., Gu L-H., Leonova J. Ye., Huisman T. H.J. Hb F-Veleta or α2Gγ240(C6)Arg→Gly. Hemoglobin 1995; 19: 407
  • Kohli-Kumar M., Zwerdling T., Rucknagel D. L. Hemoglobin F-Cincinnati, α2Gγ241(C7) Phe→Ser in a Newborn with cyanosis. Am. J. Hematol 1995; 49: 43
  • Wajcman H., Ducrocq R., Promé D., Galactéros F. Hb F-Mauritius [Aγ23 (B5) Ala deleted]: evidence for an identical hotspot for deletions in the various β-like genes. C.R. Acad. Sci. 1995; 318: 1065
  • Gu L-H., Öner C., Huisman H. The GγT chain (Gγ75; 136 Gly) in Hb F-Charlotte is the product of an Aγ gene with a limited gene conversion and that in Hb F-Waynesboro of a mutated Gγ gene. Hemoglobin 1995; 19: 413
  • Papadakis M., Drakoulakou O., Papapanagiotou E., Pessini D., Loutradi-Anagnostou A. Hb A2-Agrinio [δ43(CD2)Glu→Gly (GAG→GGG)]: A new δ chain variant detected in a Greek family. Hemoglobin 1995; 19: 295
  • Kaeda J., Jarvis M., Kokal I., Reeves J., Vulliamy T., Luzzatto L. A new double mutant Hb C-Rothschild, Abstract Book. 5th International Conference on the Thalassaemias and the Haemoglobinopathies Nicosia, Cyprus, 1993, 215
  • Wajcman H., Deon C., Prome D., Prehu C., Riou J., Galacteros F. Hb Antananarivo [α(NA1) Val→Gly]: a new variant affecting the N-terminus of the a chain. Abstract 242, The 6th International Conference on Thalassaemia and the Haemoglobinopathies, Malta, April, 1997
  • Lacerra G., De Angioletti M., Di Girolamo R., Sciorio A., Testa R., Schilirò G., Carestia C. Hb Caserta and Hb Bronte: two novel hemoglobin variants caused by alpha-2 globin gene mutations. Abstract 151, The 6th International Conference on Thalassaemia and the Haemoglobinopathies, Malta, April, 1997
  • Wajcman H., Promé D., Préhu C., Déon C., Riou J., Bouanga J. C., Papassotiriou I., Lahary A., Galactéros F. Hb Les Andelys [α83 (F4)Leu→Pro]: a new moderately unstable variant. Hemoglobin, in press
  • Brennan S. O., Matthews J. R.D. Hb Auckland [α87(F8)His→Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry. Hemoglobin, in press
  • Déon C., Riou J., Promé J-C., Galactéros F., Wajcman H., Promé D. Hemoglobin αT9 variants determined by combined methods of mass spectrometry: a new variant, Hb Villeurbanne βH89Y. Abstract P20, XIth International Conference on Methods in Protein Structure Analysis, Annecy, September, 1996
  • Wajcman H., Kister J., Riou J., Galacteros F., Girot R., Maier-Redel-Sperger M., Nayudu N. V. S., Giordano P. C. Hb Godavari [α95 (G2)Pro→Thr|: a neutral amino acid substitution in the α1β2 interface that modifies the electrophoretic mobility of hemoglobin. Hemoglobin, in press
  • Wajcman H., Kister J., Griffon N., Promé D., Davies S. C., Galactéros F., Henthorn J. S. A new Hb variant altering an important contact area: Hb West One (α 126 (H9) Asp→Gly). Ahstract 107. Br. J. Haematol. 1996; 93: 28, (Suppl. 2)
  • Harteveld C. L., Giordano P. C., Losekoot M., Heister J. G. A. M., Batelaan D., Van Delft P., Bruin M. C. A., Bernini L. F. Hb Utrecht [α2 129(H12)Leu→Pro], a new unstable α2-chain variant associated with a mild α-thalassaemic phenotype. Br. J. Haematol. 1996; 94: 483
  • Ohba Y., Hattori Y., Sakata S., Yamashiro Y., Okayama N., Hirano T., Nakanishi T., Miyazaki A., Shimizu A. Hb Niigata [β1(NA1) Val→Leu]: the fifth variant with retention of the initiator methionine and partial aceytylation. Hemoglobin 1997; 21: 179
  • Philippe M., Herman M., Irenge L., Derclaye I., Gala J. L., Heusterspreute M. Hb Agrigente [β (NA2) His→Pro]: a new β-globin chain variant found in a diabetic patient. Abstract 45, The 6th International Conference on Thalassaemia and the Haemoglobinopathies, Malta, April, 1997
  • Bianco I., Cappabianca M. P., Lerone M., Morlupi L., Rinaldi S. Hb Siirt [β27(B9)Ala→Gly]: a new, electrophoretically silent, hemoglobin variant. Hemoglobin, in press
  • Divoký V., Pospíilová D., Luhový M., Indrák K. HB-HANÁ or α2β2 63 (E7) His-Asn, a new unstable haemoglobin variant with variable clinical manifestations. Ahstract 88. Br. J. Haematol. 1996; 93: 23, (Suppl. 2)
  • Ivaldi G., Scimè-Degani V., David O., Baffico M., Baldi M., Leone D., Mazzocco M., Leone L., Piga A., Furlan E., Ricco G. A new fast-moving variant causing erythrocytosis and mild hemolysis: Hb Gambara [β82(EF6)Lys→Glu]. Hemoglobin 1997; 21: 345
  • Hoyer J. D., Wick M. J., Thibodeau S. N., Kechteiger K. S., Cook J. D., Fairbanks V. F. Hb Silver Springs [β131(H9)Gln→His], a new hemoglobin variant found in an African-American male. Hemoglobin, in press
  • De Angioletti M., Lacerra G., Gaudiano C., Mastrullo L., Colella R., Vaccaro E., Carestia C. Hb A2 Metaponto: a new delta-chain detected in the molecular screening of abnormal delta-globin alleles in Southern Italy. Abstract 150, The 6th International Conference on Thalassaemia and the Haemoglobinopathies, Malta, April, 1997
  • Rahbar S., Lee C., Fairbanks V. F., McCormick D. J., Kubik K., Madden B. J., Nozari G. Hb Watts [α74(EF3) or α75(EF4) Asp→0]: a shortened α chain variant due to the deletion of three nucleotides in exon 2 of the α2-globin gene. Hemoglobin 1997; 21: 321
  • Wajcman H., Préhu M. O., Préhu C., Blouquit Y., Promé D., Goldcher A., Galactéros F. Hemoglobin Phnom Penh [α 117Phe (Hl)-Ile-α1 18Thr(H2)]: evidence for a hotspot for insertion of residues in the third exon of the α-chain. Abstract 108. Br. J. Haematol. 1996; 93: 38, (Suppl. 2)
  • Greenberg J., Fairbanks V. F., Hoyer J., Thibodeau S. N. Hemoglobin Fairfax, a tandem duplication of β90–94 inserted between β94–95 (proved by DNA Sequence Analysis); a previously undescribed unstable hemoglobin variant associated with severe hemolytic anemia and stroke during early childhood. ASH Abstracts for 1997
  • Smetanina N. S., Gu L-H., Rodriguez Romero W. E., Howard E. F., Huisman T. H.J. The relative levels of different types of β-mRNA and β-globin in BFU-E derived colonies from patients with β chain variants; further evidence for somatic mosaicism in the Hb Costa Rica carrier [β77 (EF1)His→Arg]. Hemoglobin 1996; 20: 199
  • Bonaventura C., Arumugam M., Cashon R., Bonaventura J., Moo-Penn W. F. Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (β139 Asn→Lys) that can modulate cooperativity as well as oxygen affinity. J. Mol. Biol. 1994; 239: 561
  • Hutt P. J., Pisciotta A. V., Fairbanks V. F., Thibodeau S. N., Green M. M. DNA sequence analysis proves Hb M-Milwaukee-2 is due to β-globin gene codon 92 (CAC→TAC), the mutation postulated for Hb M-Hyde Park and Hb M-Akita. Hemoglobin, in press
  • Han J. Y., Wee J. H., Kim J. M., Kim J. Y., Kim I. H., Rodger G. P. A new observation of Hb Yamagata with a different nucleotide substitution: β132 AAA→AAT. Hemoglobin 1996; 20: 165
  • Fairbanks V. F., McCormick D. J., Kubic K., Madden B. J., Holmes M. W., Hoyer J. D. Hemoglobin Rockford, β68(E12)Leu→Phe. A new Hb variant associated with mild anemia. ASH Abstracts for 1997
  • Huisman T. H.J. Compound heterozygosity for Hb S and the hybrid Hbs Lepore, P-Nilotic, and Kenya; comparison of hematological and hemoglobin composition data. Hemoglobin 1997; 21: 249

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.