Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 18, 1994 - Issue 2
21
Views
23
CrossRef citations to date
0
Altmetric
Original Article

International Hemoglobin Information Center

Pages 77-161 | Published online: 07 Jul 2009

References

  • Crookston J. H., Beale D., Irvine D., Lehmann H. A new Haemoglobin J Toronto (â5 Alanine→Aspartic acid). Nature 1965; 208: 1059–1061
  • Sumida I., Ohta Y., Imamura T., Yanase T. Hemoglobin Sawara: â6(A4) Aspartic acid→Alanine. Biochim. Biophys. Acta 1973; 322: 23–26
  • Sasaki J., Imamura T., Sumida I., Yanase T., Ohya M. Increased oxygen affinity for Hemoglobin Sawara: âA4(6) Aspartic acid→Alanine. Biochim. Biophys. Acta 1977; 495: 183–186
  • Jue D. L., Johnson M. H., Patchen L. C., McOpenn W. F. Hemoglobin Dunn: â6(A4) Aspartic acid→Asparagine. Hemoglobin 1979; 3: 137–143
  • Pootrakul S., Kematorn B., Na-Nakorn S., Suanpan S. A new a hemoglobin variant: Haemoglobin Anantharaj alpha 11 (A9) Lysine→Glutamic acid. Biochim. Biophys. Acta 1975; 405: 161–166
  • Rosa J., Maleknia N., Vergoz D., Dunet R. Une nouvelle hemoglobine anormale: I'hemoglobin J â Paris 12 Ala→Asp. Nouv. Rev. Fr. D'Hemat. 1965; 6: 423–426
  • Trincao C, Martins De Melo J., Lorkin P. A., Lehmann H. Haemoglobin J Paris in the South of Portugal (Algarve). Acta Haematol. 1968; 39: 291–298
  • Marti H. R., Pik C, Mosimann P. Eine neue hämoglobin I variante: Hb I Interlaken. Acta Haematol. 1964; 32: 9–16
  • 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: 269–270
  • Silvestroni E., Bianco I., Tentori L., Vivaldi G., Carta S., Sorcini M., Brancati C. The structural abnormality of Hemoglobin N present in a family from Cosenza. Proc. 10th Congr. Eur. Soc. Hematol., Strasbourg, 1965. Part II. Karger, Basel, New York 1967; 232–237
  • Vella F., Casey R., Lehmann H., Labossiere A., Jones T. G. Haemoglobin Ottawa: â2 15 (A13) Gly→Arg β2. Biochim. Biophys. Acta 1974; 336: 25–29
  • Pootrakul S., Srichiyanont S., Wasi P., Suanpan S. Hemoglobin Siam â2 15 Arg β2): A new a chain variant. Humangenetik 1974; 23: 199–204
  • Beale D., Lehmann H. Abnormal haemoglobins and the genetic code. Nature 1965; 207: 259–261
  • Schneider R. G., Alperin J. B., Beale D., Lehmann H. Hemoglobin I in an American Negro family: Structural and hematologic studies. J. Lab. Clin. Med. 1966; 68: 940–946
  • 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: 816–822
  • Baur E. W. Hb â2 glu β2 (Hb I) in a Caucasian family: Independent mutation or common origin?. Humangenetik 1968; 6: 368–372; 111
  • Griffiths K. D., Lang A., Lehmann H., Mann J. R., Plowman D., Raine D. N. Haemoglobin Handsworth eâ18 (A16) Glycine→Arginine. FEBS Lett. 1977; 75: 93–95
  • Rahbar S., Ala F., Akhavan E., Nowzari G., Shoa'i I., Zamanianpoor M. H. Two new haemoglobins: Haemoglobin Perspolis [â64 (E13) Asp→Tyr] and Haemoglobin J-Kurosh [→19 (AB1) Ala→Asp]. Biochim. Biophys. Acta 1976; 27(4)119–125
  • Kendall A. G., Barr R. D., Lang A., Lehmann H. Haemoglobin J Nyanza: â21 (B2) Ala→Asp. Biochim. Biophys. Acta 1973; 10(3)357–359
  • 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 a-chain variant of hemoglobin â23 Glu NH2). J. Lab. Clin. Med. 1965; 66: 886–887
  • 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. â2 23Glu→Lys β2. Am. J. Hum. Genet. 1968; 20: 570–578
  • Marengo-Rowe A. J., Beale D., Lehmann H. New human haemoglobin variant from southern Arabia: G-Audhali (â23 (B4) Glutamic acid→Valine) and the variability of B4 in human haemoglobin. Nature 1968; 219: 1164–1166
  • Schneider R. G., Brimhall B., Jones R. T., Bryant R., Mitchell C. B., Goldberg A. I. Hb Fort Worth: â27 Glu→Gly (B8) a variant present in unusually low concentration. Biochim. Biophys. Acta 1971; 243: 164–169
  • Ahern E., Ahern V., Holder W., Palomino E., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin Spanish Town â27 Glu→Val (B8). Biochim. Biophys. Acta 1976; 427: 530–538
  • Vettore L., DeSandre G., Dilorio E. E., Winterhalter H. K., Lang A., Lehmann H. A new abnormal hemoglobin O Padova, â30 (Bll) Glu→Lys and a dyserythropoietic anemia with erythroblastic multinuclearity co-existing in the same patient. Blood 1974; 44: 869–877
  • Schneider R. G., Jim R. T.S. A new haemoglobin variant (the 'Honolulu Type') in a Chinese. Nature 1961; 190: 454–455
  • Vella F., Ager J. A. M., Lehmann H. An abnormal haemoglobin in a Chinese: Haemoglobin G. Nature 1958; 82(1)460–461
  • Swenson R. T., Hill R. L., Lehmann H., Jim R. T.S. A chemical abnormality in Hemoglobin G from Chinese individuals. J. Biol. Chem. 1962; 237: 1517–1520
  • Marinucci M., Mavilio F., Tentori L., D'Erasmo F., Colapietro A., De Stasio G., Di Fonzo S. A new human hemoglobin variant: Hb Ban â2 45(CD3) His→Gln β2). Biochim. Biophys. Acta 1980; 622: 315–319
  • Beretta A., Prato V., Gallo E., Lehmann H. Haemoglobin Torino -â43 (CD1) Phenylalanine→Valine. Nature 1968; 217: 1016–1018
  • Ohba Y., Miyaji T., Matsouka M., Yokoyama M., Numakura H., Nagata K., Takebe Y., Izumi Y., Shibata S. Hemoglobin Hirosaki (â43 [CE1] Phe→Leu), a new unstable variant. Biochim. Biophys. Acta 1975; 05(4)155–160
  • Braconnier F., Gacon G., Thillet J., Wajcman H., Soria J., Maigret P., Labie D., Rosa J. Hemoglobin Fort de France â245 (CD3) His→Arg β2) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1977; 493: 228–233
  • Sumida I. Studies of abnormal hemoglobins in Western Japan. Frequency of visible hemoglobin variants, and chemical characterization of Hemoglobin Sawara â2 6Ala β2) and Hemoglobin Mugino (Hb L Ferrara; â2 47Gly β2). Jap. J. Hum. Genet. 1975; 19: 343–363
  • 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: 484–486
  • Halbrecht I., Isaacs W. A., Lehmann H., Ben-Porat F. Hemoglobin Hasharon (a47 Aspartic acid→Histidine). Israel J. Med. ScL 1967; 3: 827–831
  • Ostertag W., Smith E. W. Hb Sinai: A new achain mutant aL47 His. Humangenetik 1968; 6: 377–379
  • Schneider R. G., Ueda S., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sealy (â2 47His β2): A new variant in a Jewish family. Am. J. Hum. Genet. 1968; 20: 151–156
  • Bianco I., Modiano G., Bottini E., Lucci R. Alteration in the â-chain of Haemoglobin L Ferrara. Nature 1963; 198: 395–396
  • Tentori L. Hemoglobin L Ferrara = Hemoglobin Hasharon. Hemoglobin 1977; 1: 602
  • Rahbar S., Mahdavi N., Nowzari G., Mostafavi I. Hemoglobin Arya â247(CD5) Aspartic acid→Asparagine. Biochim. Biophys. Acta 1975; 386: 525–529
  • 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 (â48 (CD6) Leu→Arg). Biochim. Biophys. Acta 1975; 379: 28–32
  • Tangheroni W., Zorcolo G., Gallo E., Lehmann H. Haemoglobin J Sardegna: â50 (CD8) Histidine→Aspartic acid. Nature 1968; 218: 470–471
  • 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 (â51 Gly→Asp). Nouv. Rev. Fr. D'Hemat. 1972; 12: 289–300
  • Reynolds C. A., Huisman T. H.J. Hemoglobin Russ or â2 51 Arg β2. Biochim. Biophys. Acta 1966; 130: 541–543
  • Alberti R., Mariuzzi G. M., Artibani L., Bruni E., Tentori L. A new haemoglobin variant: J-Rovigo alpha 53 (E-2) Alanine→Aspartic acid. Biochim. Biophys. Acta 1974; 342: 1–4
  • Miyaji T., Iuchi I., Takeda I., Shibata S. Hemoglobin Shimonoseki (â2 54Arg β2 A), a slow-moving hemoglobin found in a Japanese family, with special reference to its chemistry. Acta Haematol. Jap. 1963; 26: 531–536
  • Jones R. T., Brimhall B., Lisker R. Chemical characterization of Hemoglobin Mexico and Hemoglobin Chiapas. Biochim. Biophys. Acta 1968; 154: 488–495
  • Rosa J., Labie D., Maleknia N., Blum N. Sur quelques hemoglobines anormales nouvelles recemment isolees en France. International Symposium on Comparative Hemoglobin Structure. Thessaloniki April 11-13, 1966; 140–145
  • Fessas Ph., Kaltsoya A., Loukopoulos D., Nilsson L.-O. On the chemical structure of Haemoglobin Uppsala. Hum. Hered. 1969; 19: 152–158
  • Pootrakul S., Boonyarat D., Kematorn B., Suanpan S., Wasi P. Hemoglobin Thailand a56 (E5) Lys→Thr]: A new abnormal human hemoglobin. Hemoglobin 1977; 1: 781–798
  • Rahbar S., Kinderlerer J. L., Lehmann H. Haemoglobin L Persian Gulf: â57 (E6) Glycine→Arginine. Acta Haematol. 1969; 42: 169–175
  • Baglioni C. A chemical study of Hemoglobin Norfolk. J. Biol. Chem. 1962; 237: 69–74
  • Imamura T. Hemoglobin Kagoshima: An example of Hemoglobin Norfolk in a Japanese family. Am. J. Hum. Genet. 1966; 18: 584–593
  • Yanase T., Hanada M., Seita M., Ohya I., Ohta Y., Imamura T., Fujimura T., Kawasaki K., Yamaoka K. Molecular basis of morbidity -From a series of studies of hemoglobinopathies in Western Japan. Jap. J. Hum. Genet. 1968; 13: 40–53
  • Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl. Acad. Sci., USA 1961; 47: 1758–1767
  • Shimizu A., Hayashi A., Yamamura Y., Tsugita A., Kitayama K. The structural study on a new hemoglobin variant, Hb M Osaka. Biochim. Biophys. Acta 1965; 97: 472–482
  • Hansen H. A., Jagenburg O. R., Johansson B. G. Studies on an abnormal hemoglobin causing hereditary congenital cyanosis. Acta Paediatr. 1960; 49: 503–511
  • Hollan S. R., Szelenyi J. G., Lehmann H., Beale D. A Boston-type Haemoglobin M in Hungary: Haemoglobin M Kiskunhalas. Haematologia 1967; 1: 11–18
  • Barclay G. P. T., Charlesworth D., Lehmann H. Abnormal haemoglobin in Zambia. A new Haemoglobin Zambia â60 (E9) Lysine→Asparagine. Br. Med. J. 1969; 4: 595–596
  • Brimhall B., Duerst M., Hollan S. R., Stenzel P., Szelenyi J., Jones R. T. Structural characterizations of Hemoglobins J Buda (â61 (E10) Lys→Asn) and G Pest (â74 (EF3) Asp→Asn). Biochim. Biophys. Acta 1974; 336: 344–360
  • Thillet J., Blouquit Y., Perrone F., Rosa J. Hemoglobin Pontoise â63 Ala→Asp (E12). A new fast moving variant. Biochim. Biophys. Acta 1977; 491: 16–22
  • Blackwell R. Q., Jim R. T. S, Tan T. G. H, Weng M.-l., Liu C.-S., Wang C-L. Hemoglobin G Waimanalo: â64 Asp→Asn. Biochim. Biophys. Acta 1973; 322: 27–33
  • Ramot B., Kinderlerer J. B., Lehmann H. Cited in WHO Technical Report Series No. 509. Annex l, Geneva 1972
  • Sukumaran P. K., Merchant S. M., Desai M. P., Wiltshire B. G., Lehmann H. Haemoglobin Q India (â64(E13) Aspartic acid→Histidine) associated with β-thalassemia observed in three Sindhi families. J. Med. Genet. 1972; 9: 436–442
  • Miyaji T., Iuchi I., Yamamoto K., Ohba Y., Shibata S. Amino acid substitution of Hemoglobin Ube 2 (â2 68 Asp β2): An example of successful application of partial hydrolysis of peptide with 5% acetic acid. Clin. Chim. Acta 1967; 16: 347–352
  • 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
  • Chernoff A. I., Pettit N., Jr. The amino acid composition of hemoglobin. VI. Separation of the tryptic peptides of Hemoglobin Knoxville No. 1 on Dowex-1 X-2 and Sephadex. Biochim. Biophys. Acta 1965; 97: 47–60
  • Bowman B., Barnett D. R., Hodgkinson K. T., Schneider R. G. Chemical characterization of Haemoglobin G St-1. Nature 1966; 211: 1305–1306
  • Minnich V., Cordonnier J. K., Williams W. J., Moore C. V. Alpha, beta and gamma hemoglobin polypeptide chains during the neonatal period with description of a fetal form of Hemoglobin D St. Louis. Blood 1962; 19: 137–167
  • Dance N., Huehns E. R., Shooter E. M. The chemical Investigation of Haemoglobin G Bristol and G Bristol\C. Biochim. Biophys. Acta 1964; 86: 144–148
  • Colombo B., Vidal H., Kamuzora H., Lehmann H. A new Haemoglobin J-Habana â71 (E20) Alanine→Glutamic acid. Biochim. Biophys. Acta 1974; 351: 1–6
  • Rahbar S., Nowzari G., Daneshmand P. Hemoglobin Daneshgah Tehran â2 72 (EF1) Histidine-Arginine β2A. Nature New Biol. 1973; 45(2)268–269
  • Pootrakul S., Dixon H. G. Hemoglobin Mahidol: A new hemoglobin a-chain mutant. Can. J. Biochem. 1970; 48: 1066–1078
  • Blackwell R. Q., Liu C.-S. Hemoglobin G Taichung: a74 Asp→His. Biochim. Biophys. Acta 1970; 200: 70–75
  • Lorkin P. A., Charlesworth D., Lehmann H., Rahbar S., Tuchinda S., Lie-Lnjo L. E. Two Haemoglobins Q, â74 (EF3) and â75 (EF4) Aspartic acid→ Histidine. Br. J. Haematol. 1970; 19: 117–125
  • Orringer E. P., Wilson J. B., Huisman T. H.J. Hemoglobin Chapel Hill or â2 74 Asp→Gly β2;. FEBSlett. 1976; 65: 297–300
  • Vella F., Wiltshire B., Lehmann H., Galbraith P. Hemoglobin Winnipeg â2 75 Asp-Tyr β2. Clin. Biochem. 1973; 6: 66–70
  • 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: 383–388
  • Van Ros G., Beale D., Lehmann H. Haemoglobin Stanleyville-11 (â78 Asparagine→Lysine). Br. Med. J. 1968; 4: 92–93
  • Rucknagel D. L., Brandt N. J., Spencer H. H. â-Chain mutants of human hemoglobin contributing to the genetics of the a-chain locus. Proc. 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: 1427–1429
  • Honig G. R., Shamsuddin M., Tremaine L. M., Mason R. G., Vida L. N., Sarnwick R., Shahidi N. T. Hemoglobin Nigeria (a81 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 â82 Ala→Asp. Clin. Res. 1978; 26: 22A
  • Crookston J. H., Farquharson H. A., Beale D., Lehmann H. Hemoglobin Etobicoke: â84 (F5) Serine replaced by Arginine. Can. J. Biochem. 1969; 47: 143–146
  • Huehns E. R. The unstable hemoglobins. Bull. Soc. Chem. Biol 1970; 52: 1131–1146
  • Lorkin P. A., Huntsman R. G., Ager J. A. M., Lehmann H., Vella F., Darbre P. D. Haemoglobin G Norfolk: â85 (F6) Asp→Asn. Biochim. Biophys. Acta 1975; 379: 22–27
  • Cohen-Solal M., Manasse B., Thillet J., Rosa J. Haemoglobin G Norfolk â85 (F6) Asp→Asn. Structural characterization by sequenator analysis and functional properties of a new variant with high oxygen affinity. FEBS Lett. 1975; 50: 163–167
  • Fujiwara N., Maekawa T., Matsuda G. Hemoglobin Atago (â2 85 Tyr β2) a new abnormal human hemoglobin found in Nagasaki. Int. J. Protein Res. 1971; 3: 35–39
  • Reed R. E., Winter W. P., Rucknagel D. L. Haemoglobin Inkster (â2 85 Aspartic acid→Valine \32) coexisting with \3-thalassemia in a Caucasian family. Br. J. Haematol. 1974; 26: 475–484
  • Knuth A., Pribilla W., Marti R. H., Winterhalter K. H. Hemoglobin Moabif. Alpha 86 (F7) Leu→Arg. A new unstable abnormal hemoglobin. Acta Haematol. 1979; 61: 121–124
  • Miyaji T., Iuchi I., Shibata S., Takeda I., Tamura A. Possible amino acid substitution in the â-chain (â87 Tyr) of Hb M Iwate. Acta Haematol. Jap. 1963; 26: 538–543
  • Heller P., Weinstein H. G., Yakulis V. J., Rosenthal I. M. Hemoglobin M Kankakee, a new variant of Hemoglobin M. Blood 1962; 20: 287–301
  • 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 â non encore decrite, dans une famille Francaise. Compt. R. Sceanc. Soc. Biol 1966; 160: 2270–2272
  • Vella F., Charlesworth D., Lorkin P. A., Lehmann H. Hemoglobin Broussais â90 Lys→Asn. Can. J. Biochem. 1970; 48: 908–910
  • Braconnier F., Cohen-Solal M., Schlegel N., Blouquit Y., Thillet J., Cassius De Linval J., Rosa J., Hemoglobin J. Broussais â2 90 Lys→Asn β2A (FG2), decouverte dans une famille Martiniquaise. Nouv. Rev. Fr. D'Hemat., 15: 333–342
  • Hyde R. D., Kinderlerer J. L., Lehmann H., Hall M. D. Haemoglobin J Rajappen: â90 (FG2) Lys→Thr. Biochim. Biophys. Acta 1971; 243: 515–519
  • Brennan S. O., Tauro G. P., Melrose W., Carrell R. W. Haemoglobin Port Phillip â91 (FG3) Leu→Pro. A new unstable haemoglobin. FEBSLett. 1977; 81: 115–117
  • Botha M. C., Beale D., Isaacs W. A., Lehmann H. Haemoglobin J Cape Town 2 â92 Argimne→Glutamine β2. Nature 1966; 212: 792–795
  • Lines J. G., McIntosh R. Oxygen binding by Haemoglobin J Cape Town (â2 92 Arg→Gln). Nature 1967; 15(2)297–298
  • Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the â and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol. 1966; 19: 91–108
  • Charache S., Weatherall D. J., Clegg J. B. Polycythemia associated with a hemoglobinopathy. J. Clin. Invest. 1966; 45: 813–822
  • Wajcman H., Belkhodja O., Labie D. Hb Setif: Gl (94) âAsp→Tyr. A new aL chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits. FEBS Lett. 1972; 27: 298–300
  • Schneider R. G., Atkins R. J., Hosty T. S., Tomlin G., Casey R., Lehmann H., Lorkin P. A., Nagai K. Haemoglobin Titusville: â94 Asp→Asn, a new haemoglobin with a lowered affinity for oxygen. Biochim. Biophys. Acta 1975; 400: 365–373
  • Schroeder W. A., Shelton B. J., Shelton J. R., Powars D. Hemoglobin Sunshine Seth -â2 (94(G1) Asp→His) β2. Hemoglobin 1979; 3: 145–159
  • Huisman T. H. J., Adams H. R., Wilson J. B., Efremov G. D., Reynolds C. A., Wrightstone R. N. Hemoglobin G Georgia or â2 95 Leu (G2) β2. Biochim. Biophys. Acta 1970; 200: 578–580
  • 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 (â2 95 (G2) 02) and Rampa (β2 95 Ser (G2) β2). J. Biol. Chem. 1972; 247: 1433–1439
  • De Jong W. W. W., Bernini L. F., Meera Khan P. Haemoglobin Rampa: a95 Pro→Ser. Biochim. Biophys. Acta 1971; 236: 197–200
  • Wiltshire B. G., Clark K. G. A., Lorkin P. A., Lehmann H. Haemoglobin Denmark Hill â95 (G2) Pro→Ala, a variant with unusual electrophoretic and oxygen binding properties. Biochim. Biophys. Acta 1972; 278: 459–464
  • 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 â2 95 Arg (G2) β2. Eur. J. Biochem. 1972; 29: 301–307
  • Crookston J. H., Farquharson H. A., Kinderlerer J. L., Lehmann H. Hemoglobin Manitoba: âl02 (G9) Serine replaced by Arginine. Can. J. Biochem. 1970; 48: 911–914
  • Sanguansermsri T., Matragoon S., Changloah L., Flatz G. Hemoglobin Suan-Dok (â2 109 (G16) Leu→Arg β2): An unstable variant associated with â-thalassemia. Hemoglobin 1979; 3: 161–174
  • Charache S., Ostertag W. Hemoglobin Hopkins-2 ((âll2 Asp) 2 β2): “Low output” protects from potentially harmful effects. Blood 1970; 36: 852
  • Clegg J. B., Charache S. The structure of Hemoglobin Hopkins-2. Hemoglobin 1978; 2: 85–88
  • Niazi G. A., Efremov G. D., Nikolov N., Hunter E., Jr., Huisman T. H.J. Hemoglobin Strumica or â2 112(G19) His→Arg β2. (With an addendum: Hemoglobin J Paris-I â2 12 (A10) Ala→Asp β2 in the same population.). Biochim. Biophys. Acta 1975; 12(4)181–186
  • Beksedic D., Rajevska T., Lorkin P. A., Lehmann H. Hb Serbia (â112(G19) His→Arg), a new haemoglobin variant from Yugoslavia. FEBSLett. 1975; 58: 226–229
  • Gajdusek D. C., Guiart J., Kirk R. L., Carrell R. W., Irvine D., Kynoch P. A. M., Lehmann H. Haemoglobin J Tongariki (â 115 Alanine→Aspartic acid): the first new haemoglobin variant found in a Pacific (Melanesian) population. J. Med. Genet. 1967; 4: 1–6
  • Baglioni C, Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229–232
  • Lie-Lnjo L. E. Sadono Haemoglobin O (Buginese X) in Sulawesi. Br. Med. J. 1958; 1: 1461–1462
  • Sansone G., Centa A., Sciarratta V., Gallo E., Lehmann H. Haemoglobin O Indonesia (â116 Glu→Lys) in an Italian family. Acta Haematol 1970; 43: 40–47
  • Ohba Y., Miyaji T., Matsuoka M., Morito M., Iuchi I. Characterization of Hb Ube-4: Alpha 116 (GH4) Glu→Ala. Hemoglobin 1978; 2: 181–186
  • Blackwell R. Q., Wong Hock Boon, Wang C.-L., Weng M.-l., Liu C.-S. Hemoglobin J Meerut: â120 Ala→Glu. Biochim. Biophys. Acta 1974; 351: 7–12
  • Kamuzora H., Lehmann H., Griffiths K. D., Mann J. R., Raine D. N. Anew haemoglobin variant Hemoglobin J Birmingham â 120 (H3) Ala→Glu. Ann. Clin. Biochem. 1974; 11: 53–55
  • Moo-Penn W. F., Jue D. L., Johnson M. H., Wilson S. M., Therrel B., Jr., Schmidt R. M. Hemoglobin Tarrant: â 126 (H9) Asp→Asn. A new hemoglobin variant in the a1β1 contact region showing high oxygen affinity and reduced cooperativity. Biochim. Biophys. Acta 1977; 490: 443–451
  • Vella F., Galbraith P., Wilson J. B., Wong S. C., Folger G. C., Huisman T. H.J. Hemoglobin St. Claude or â2 127 (H10) Lys→Thr β2. Biochim. Biophys. Acta 1974; 365: 318–322
  • Moo-Penn W. F., Bechtel K. C., Johnson M. H., Jue D. L., Holland S., Huff C, Schmidt R. M. Hemoglobin Jackson, al27 (H10) Lys→Asn. Am. J. Clin. Pathol. 1976; 66: 453–456
  • 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 â2 136 Pro β2, an unstable a-chaln abnormal hemoglobin. Biochim. Biophys. Acta 1968; 154: 220–222
  • Clegg J. B., Weatherall D. J., Wong Hock Boon, Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 222: 379–380
  • Poyart C., Krishnamoorthy R., Bursaux E., Gacon G., Labie D. Structural and functional studies of Haemoglobin Suresnes or â2 141 (HC3) Arg→His β2, a new high oxygen affinity mutant. FEBSLett. 1976; 69: 103–107
  • 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 (â2141 (HC3) Arg→Ser β2). Biochim. Biophys. Acta 1977; 494: 48–50
  • Mavilio F., Marinucci M., Tentori L., Fontanarosa P. P., Rossi U., Biagiotti S. Hemoglobin Legnano (â2 141 (HC3) Arg→Leu β2): A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1978; 2: 249–259
  • Martinez G., Lima F., Residenti C, Colombo B. Hb J Camagüey â2141 (HC3) Arg→Gly β2-A new abnormal human hemoglobin. Hemoglobin 1978; 2: 47–52
  • Moo-Penn W. F., Bechtel K. C., Schmidt R. M., Johnson M. H., Jue D. L., Schmidt D. E., Jr., Dunlap W. M., Opella S. J., Bonaventura J., Bonaventura C. Hemoglobin Raleigh (β1 Valine→Acetylalanine). Structural and functional characterization. Biochemistry 1977; 16: 4872–4879
  • Labossiere A., Vella F., Hiebert J., Galbraith P. Hemoglobin Deer Lodge: â2 β2 His→Arg. Clin. Biochem. 1972; 5: 46–50
  • Ingram V. M. Abnormal human haemoglobins, in. the chemical difference between normal and sickle cell haemoglobins. Biochim. Biophys. Acta 1959; 36: 402–411
  • 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: 409–421
  • Blackwell R. Q., Oemijati S., Pribadi W., Weng M.-L, Liu C.-S. Hemoglobin G Makassar: β6 Glu→Ala. Biochim. Biophys. Acta 1970; 214: 396–401
  • Hill R. L., Swenson R. T., Schwartz H. C. Characterization ofa chemical abnormality in Hemoglobin G. J. Biol. Chem. 1960; 235: 3182–3187
  • 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: 1583–1585
  • Bonaventura J., Riggs A. Polymerization of hemoglobins of mouse and man. Structural basis. Science 1967; 158: 800–802
  • Tondo C. V., Bonaventura J., Bonaventura C, Brunori M., Antonini E. Functional properties of Hemoglobin Porto Alegre (â2Aβ2 Ser→Cys) and the reactivity of its extra cysteinyl residue. Biochim. Biophys. Acta 1974; 342: 15–20
  • Arcasoy A., Casey R., Lehmann H., Cavdar A. O., Berki A. A new Haemoglobin J from Turkey -Hb Ankara (β10 (A7) Ala→Asp). FEBS Lett. 1974; 42: 121–123
  • Monn E., Gaffney P. J., Lehmann H. Haemoglobin Sögn(β14 Arginine). Anew haemoglobin variant. Scand. J. Haematol. 1968; 5: 353–360
  • Beuzard Y., Basset P., Braconnier F., El Gammel H., Martin L., Oudard J. L., Thillet J. Haemoglobin Saki âβ2 14 Leu→Pro (All) structure and function. Biochim. Biophys. Acta 1975; 393: 182–187
  • Milner P. F., Corley C. C., Pomeroy W. L., Wilson J. B., Gravely M., Huisman T. H.J. Thalassemia intermedia caused by heterozygosity for both β-thalassemia and Hemoglobin Saki (β14 (All) Leu→Pro). Am. J. Hematol 1976; 1: 283–292
  • 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: 324–326
  • Gacon G., Wajcman H., Labie D., Varet B., Christoforov B. A second case of Haemoglobin Belfast (β15 [A12] Trp→Arg) observed in a French patient. Acta Haematol. 1976; 55: 313–319
  • Baglioni C, Weatherall D. J. Abnormal human hemoglobins. IX. Chemistry of Hemoglobin J Baltimore. Biochim. Biophys. Acta 1963; 78: 637–643
  • Weatherall D. J. Hemoglobin J (Baltimore) coexisting in a family with Hemoglobin S. Johns Hopkins Hosp. Bull 1964; 114: 1–12
  • 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: 368–372
  • Wong SC, Bouver N., Wilson J. B., Huisman T. H.J. Hb J Georgia = Hb J Baltimore = âtbT2 16 Gly→Asp. Clin. Chim. Acta 1971; 35: 521–522
  • Wade P. T., Jenkins T., Huehns E. R. Haemoglobin variant in a Bushman: Haemoglobin Dβ-Bushmanâβ216Gry→Arg. Nature 1967; 216: 688–690
  • Maekawa M., Maekawa T., Fujiwara N., Tabara K., Matsuda G. Hemoglobin Nagasaki: aÂ2β2 17 Glu. A new abnormal human hemoglobin found in one family in Nagasaki. Int. J. Prot. Res. 1970; 11: 147–156
  • Elion J., Belkhodja O., Wajcman H., Labie D. Two variants of Hemoglobin D in the Algerian population: Hemoglobin D Ouled Rabah β19 (Bl) Asn→Lys and Hemoglobin D Iran β22 (B4) Glu→Gln. Biochim. Biophys. Acta 1973; 310: 360–364
  • Lam H., Wilson J. B., Harris H., Gravely M., Huisman T. H.J. Hemoglobin Alamo [â2β2 19 (Bl) Asn→Asp]. Hemoglobin 1977; 1: 703–706
  • Stamatoyannopoulos G., Nute P. E., Adamson J. W., Bellingham A. J., Funk D., Hornung S. Hemoglobin Olympia (β20 Valine→Methionine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J. Clin. Invest. 1973; 52: 342–349
  • Vella F., Lorkin P. A., Carrell R. W., Lehmann H. A new hemoglobin variant resembling Hemoglobin E. Hemoglobin E Saskatoon: β22 Glu→Lys. Can. J. Biochem. 1967; 45: 1385–1391
  • Blackwell R. Q., Yang H. J., Wang C. C. Hemoglobin G Taipei: â2β2 22 Glu-Gly. Biochim. Biophys. Acta 1969; 175: 237–241
  • Vella F., Isaacs W. A., Lehmann H. Hemoglobin G Saskatoon: β22 Glu→AIa. Can. J. Biochem. 1967; 45: 351–353
  • 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: â2β2 22 Glu→Ala. Science 1968; 161: 381–382
  • Bowman B. H., Barnett D. R., Hite R. Hemoglobin G Coushatta: a beta variant with â delta-like substitution. Biochem. Biophys. Res. Commun. 1967; 26: 120, 466–470
  • 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. â2β2 22 Glu-AIa. Am. J. Phys. Anthropol 1969; 30: 389–392
  • Rahbar S. Haemoglobin D Iran: β22 Glutamic acid→Glutamine (B4). Br. J. Haematol. 1973; 24: 31–35
  • Garel M. C., Blouquit Y., Arous N., Rosa J. Hb Strasbourg âβ2 20 (B2) Val→Asp: A variant at the same locus as Hb Olympia β20 Val→Met. FEBS Lett. 1976; 72: 1–4
  • Forget B. G. Nucleotide sequence of human 0 globin messenger RNA. Hemoglobin 1977; 1: 879–881
  • 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. BiocMm. Biophys. Acta 1968; 33: 1004–1011
  • 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) #-Glycine→Valine): An unstable variant causing anemia with inclusion bodies. \. Clin. Invest. 1971; 50: 650–659
  • Idelson L. I., Didkowsky N. A., Casey R., Lorkin P. A., Lehmann H. New unstable haemoglobin (Hb Moscva, (β24 (B6) Gly→Asp) found in the U.S.S.R. Nature 1974; 249: 768–770
  • Blackwell R. Q., Liu C.-S. Hemoglobin G Taiwan-Ami â202 25 Gly→Arg. Biochem. Biophys. Res. Commun. 1968; 30: 690–696
  • Hunt J. A., Ingram V. M. Abnormal human haemoglobins. VI. the chemical difference between Haemoglobins A and E. Biochim. Biophys. Acta 1961; 49: 520–536
  • Blouquit Y., Arous N., Machado P. E. A., Garel M. C. Hb Henri Mondor: β 26 (B8) Glu→Val: A varant with a substitution localized at the same position as that of Hb E β 26 Glu-Lys. FEBS Lett. 1976; 72: 5–7
  • Idelson L. I., Didkowsky N. A., Filippova A. V., Casey R., Kynoch P. A. M., Lehmann H. Haemoglobin Volga, β 27 (B9) Ala→Asp, a new highly unstable haemoglobin with a suppressed charge. FEBS Lett. 1975; 58: 122–125
  • 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 âβ2 27 (B9) Ala→Asp: An unstable hemoglobin variant in three generations of a Dutch family. Biochim. Biophys. Acta 1976; 439: 63–69
  • Cohen-Solal M., Seligmann M., Thillet J., Rosa J. Haemoglobin Saint Louis β 28 (B10) Leucine-KSlutamine. A new unstable haemoglobin only present in a ferri form. Abstract 408, XTV Intl. Cong. Hematol., Sao Paulo, 1972. FEBS Lett. 1973; 33: 37–41
  • Thillet J., Cohen-Solal M., Seligmann M., Rosa J. Functional and physicochemical studies of Hemoglobin St.: Louis β 28 (B10) Leu→Gln. J. Clin. Invest. 1976; 58: 1β–1106
  • Sansone G., Carrell R. W., Lehmann H. Haemoglobin Genova: β 28 (B10) Leucine→Proline. Nature 1967; 214: 877–879
  • Schmidt R. M., Bechtel K. C., Johnson M. H., Thrrell B. J., Jr., Moo-Penn W. F. Hemoglobin Lufkin: →29 (Bll) Gly→Asp: An unstable hemoglobin variant involving an internal amino acid residue. Hemoglobin 1977; 1: 799–814
  • Brimhall B., Jones R. T., Baur E. W., Motulsky A. G. Structural characterization of Hemoglobin Tacoma. Biochemistry 1969; 8: 2125–2129
  • Jackson J. M., Yates A., Huehns E. R. Haemoglobin Perth: β 32 (B14) Leu→Pro. An unstable haemoglobin causing haemolysis. Br. J. Haematol 1973; 25: 607–610
  • Honig G. R., Green D., Shamsuddin M., Vida L. N., Mason R. G., Gnarra D. J., Maurer H. S. Hemoglobin Abraham Lincoln, β 32 (B14) Leucine→Proline. An unstable variant producing severe hemolytic disease. J. Clin. Invest. 1973; 52: 1746–1755
  • Garel M. C., Blouquit Y., Rosa J. Hemoglobin Castilla β 32 (B14) Leu→Arg: A new unstable variant producing severe hemolytic disease. FEBS Lett. 1975; 58: 145–147
  • Rieder R. F., Oski F. A., Clegg J. B. Hemoglobin Philly (β 35 Tyrosine→ Phenylalanine): Studies in the molecular pathology of hemoglobin. J. Clin. Invest. 1969; 48: 1627–1642
  • Yamaoka K. Hemoglobin Hirose: â2β 2 37 (C3) Tryptophan yielding-Serine. Blood 1971; 38: 730–738
  • Gacon G., Belkhodja O., Wajcman H., Labie D. Structural and functional studies of Hb Rothschild β 37 (C3) Trp→Arg. A new variant of the â, β2 contact. FEBS Lett. 1977; 82: 243–246
  • Brimhall B., Jones R. T., Schneider R. G., Hosty T. S., Tomlin G., Atkins R. Two new hemoglobins: Hemoglobin Alabama (β 339 (C5) Gln→Lys) and Hemoglobin Montgomery (β 48 (CD6) Leu→Arg). Biochim. Biophys. Acta 1975; 379: 28–32
  • Kendall A. G., Pas A. T., Wilson J. B., Cope N., Bolch K., Huisman T. H.J. Hb Vaasa or â2β 2 (39 (C5) Gln→Glu), a mildly unstable variant found in a Finnish family. Hemoglobin 1977; 1: 292–295
  • Brown W. J., Niazi G. A., Jayalakshmi M., Abraham E. C., Huisman T. H.J. Hemoglobin Athens-Georgia, or â β 40 (C6) Arg→Lys, a hemoglobin variant with an increased oxygen affinity. Biochim. Biophys. Acta 1976; 439: 70–76
  • 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 al→2 contact region. Arch. Biochem. Biophys. 1977; 179: 86–94
  • Burkett L. B., Sharma V. S., Pisciotta A. V., Ranney H. M., Bruckheimer S. Hemoglobin Mequon β 41 (C7) Phenylalanine→Tyrosine. Blood 1976; 48: 645–651
  • Dacle J. V., Shinton N. K., Gaffney P. J., Jr., Carrell R. W., Lehmann H. Haemoglobin Hammersmith (β 42 (CD1) Phe-Ser). Nature 1967; 216: 663–665
  • Ohba Y., Miyaji T., Matsuoka M., Yamaguchi K., Yonemitsu H., Ishii T., Shibata S. Hemoglobin Chiba: Hb Hammersmith in a Japanese girl. Acta Haematol. Jap. 1975; 38: 53–58
  • Keeling M. M., Ogden L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitcens J. L., Huisman T. H.J. Hemoglobin Louisville (β 42 (CD1) Phe→Leu): An unstable variant causing mild hemolytic anemia. J. Clin. Invest. 1971; 50: 2395–2402
  • Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemoglobin Bucure. sti β 42 (CD1) Phe→Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. Biophys. Acta 1971; 251: 1–6
  • Bowman B. H., Oliver C. P., Barnett D. R., Cunningham J. R., Schneider R. G. Chemical characterization of three Hemoglobins G. Blood 1964; 23: 193–199
  • Iuchi I., Ueda S., Hidaka K., Shibata S. Hemoglobin Hoshida β 43 (CD2) Glu→Gln), a new hemoglobin variant discovered in Japan. Hemoglobin 1978; 2: 235–247
  • Allan N., Beale D., Irvine D., Lehmann H. Three Haemoglobins K: Woolwich, an abnormal, Cameroon and Ibadan, two unusual variants of human Haemoglobin A. Nature 1965; 208: 658–661
  • Sick K., Beale D., Irvine D., Lehmann H., Goodall P. T., MacDougall S. Haemoglobin G Copenhagan and Haemoglobin J Cambridge. Two new \β -chain variants of Haemoglobin A. Biochim. Biophys. Acta 1967; 40(1)231–242
  • Marinucci M., Mavilio F., Tentori L., Alberti R. Hemoglobin Gavello âβ2 47 (CD6) Asp→Gly, a new hemoglobin variant from Polesine (Italy). Hemoglobin 1977; 1: 771–779
  • Rahbar S., Nowzari G., Ala F. Haemoglobin Avicenna β 47 (CD6) Asp→Ala), a new abnormal haemoglobin. Biochim. Biophys. Acta 1979; 76(5)466–470
  • Charache S., Brimhall B., Milner P., Cobb L. Hemoglobin Okaloosa (β 48 (CD7) Leucine→Arginine). An unstable hemoglobin with decreased oxygen affinity. J. Clin. Invest. 1973; 52: 2858–2864
  • Labossiere A., Hill J. R., Vella F. A new β Tp V hemoglobin variant: Hb Edmonton. Clin. Biochem. 1971; 4: 114–117
  • Jones R. T., Koler R. D., Duerst M. L., Dhindsa D. S. Hemoglobin Williamette [âβ2 51 Pro→Arg (D2)] a new abnormal human hemoglobin. Hemoglobin 1976; 1: 45–57
  • Konotey-Ahulu F. I. D., Kinderlerer J. L., Lehmann H., Ringelhann B. Haemoglobin Osu-Christiansborg: A new β -chain variant of Haemoglobin A (β 52 (D3) Aspartic acid→Asparagine) in combination with haemoglobin S. J. Med. Gent. 1971; 8: 302–305
  • Beresford C. H., Clegg J. B., Weatherall D. J. Haemoglobin Ocho Rios (β 52 (D3) Aspartic acid→Alanine); a new β -chain variant of Haemoglobin A found in combination with Haemoglobin S. \. Med. Genet. 1972; 9: 151–153
  • Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the â and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol. 1966; 19: 91–108
  • Blackwell R. Q., Liu C.-S. The identical structural anomalies of Hemoglobins J Meinung and J Korat. Biochem. Biophys. Res. Commun. 1966; 24: 732–738
  • Blackwell R. Q., Liu C.-S., Lie-Lnjo L. E., Pribadi W. Fast hemoglobin variant in Minahassan people of Sulawesi, Chinese and Thais: â2β2 56 Gly→Asp. Am. J. Phys. Anthropol 1970; 32: 147–150
  • Rahbar S., Nowzari G., Haydari H., Daneshmand P. Haemoglobin Hamadan â2β 2 56 Glycine→Arginine (D7). Biochim. Biophys. Acta 1975; 379: 645–648
  • Giardina B., Brunori M., Antonini E., Tentori L. Properties of Hemoglobin G Ferrara (β 57 (El) Asn→Lys). Biochim. Biophys. Acta 1978; 534: 1–6
  • Marengo-Rowe A. J., Lorkin P. A., Gallo E., Lehmann H. Haemoglobin Dhofar -a new variant from Southern Arabia. Biochim. Biophys. Acta 1968; 168: 58–63
  • Boulton F. E., Huntsman R. G., Lehmann H., Lorkin P., Romero Herrera A. Myoglobin variants. Br. J. Haematol. 1971; 20: 671–672
  • Blackwell R. Q., Liu C.-S., Shih T.-B. Hemoglobin J Kaohsiung: β 59 Lys→Thr. Biochim. Biophys. Acta 1971; 229: 343–348
  • 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: 469–473
  • Wajcman H., Amegnizin K. P. E, Belkhodja O., Labie D. Hemoglobin J Lome β 59 (E3) Lys→Asn. A new fast moving variant found in a Togolese. FEBS Lett. 1977; 84: 372–374
  • Kagimoto T., Morino Y., Kishimoto S. A new hemoglobin variant Hb Yatsushiro â2Aβ2 60 Val-Leu. Biochim. Biophys. Acta 1978; 532: 195–198
  • Jones R. T., Brimhall B., Huehns E. R., Motulsky A. G. Structural characterization of Hemoglobin N Seattle: â2Aβ2 61 Lys→Glu. Biochim. Biophys. Acta 1968; 154: 278–283
  • Shibata S., Miyaji T., Iuchi L, Ueda S., Takeda I. HemoglobinHikari (â2Aβ 2 61 Asp→NH2): A fast moving hemoglobin found in two unrelated Japanese families. Clin. Chim. Acta 1964; 10: 101–105
  • Beutler E., Lang A., Lehmann H. Hemoglobin Duarte: â2β 2 62 (E6) Ala→Pro: A new unstable hemoglobin with increased oxygen affinity. Blood 1974; 43: 527–535
  • Muller C. J., Kingma S. Haemoglobin Zürich â2Aβ 2 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: 1758–1767
  • Shibata S., Miyaji T., Iuchi I., Ueda S. A comparative study of Hemoglobin M Iwate and Hemoglobin M Kurume by means of electrophoresis, chromatography and analysis of peptide chains. Acta Haematol. Jap. 1961; 24: 486–494
  • Murawski K., Szymanowska Z., Kozlowska J. A new variant of abnormal methaemoglobin: Hb M Radom. Biochim. Biophys. Acta 1963; 69: 442–444
  • Hobolth N. Haemoglobin M Arhus: I. Clinical family study. Acta Paediatr. Scand. 1965; 54: 357–362
  • Josephson A. M., Weinstein H. G., Yakulis V. J., Singer L., Heller P. A new variant of Hemoglobin M disease: Hemoglobin M Chicago. J. Lab. Clin. Med. 1962; 59: 918–925
  • Betke K., Gröschner E., Bock K. Properties of a further variant of Haemoglobin M. Nature 1960; 188: 864–865
  • Hörlein H., Weber G. Über chronishe fämiliare methämoglobinämie und eine neue modifikation des methamoglobins. Deutsche Medizinische Wochenschrift 1948; 73: 476–478
  • Efremov G. D., Huisman T. H. J., Stanulovic M., Zurovec M., Duma H., Wilson J. B., Jeremic V. Haemoglobin M Saskatoon and Haemoglobin M Hyde Park in two Yugoslavian families. Scand. J. Haematol. 1974; 13: 48–60
  • Kohne E., Grosze H. P., Versmold H., Kley H. P., Kleihauer E. Hb M Erlangenâ2β 2 63 (E7) Tyr. Eine neue mutation mit hamolyse und diaphorasemangel. Kinderheilk 1975; 120: 69–78
  • Wajcman H., Krishnamoorthy R., Gacon G., Elion J., Allard C, Labie D. A nw hemoglobin variant involving the distal histidine: Hb Bicětre (β 63 (E7) His→Pro). J. Mol. Med. 1976; 1: 187–197
  • 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: β 65 (E9) Lys→n, a beta homologue of Hb Zambia. FEBS Lett. 1974; 39: 200–204
  • Garel M. C., Hassan W., Coquelet M. T., Goossens M., Rosa J. Hemoglobin J Cairo: β 65 (E9) Lys→Gln, a new hemoglobin variant discovered in an Egyptian family. Biochim. Biophys. Acta 1976; 20(4)97–104
  • Rosa J., Labie D., Wajcman H., Boigne J. M., Cabannes R., Bierme R., Ruffle J. Haemoglobin I Toulouse: β 66 (E10) Lys→Glu: A new abnormal haemoglobin with a mutation localized on the E10 porphyrin surrounding zones. Nature 1969; 223: 190–191
  • Steadman J. H., Yates A., Huehns E. R. Idiopathic Heinz body anaemia: Hb-Bristol (β 67 (Ell) Val-Asp). Br. J. Haematol. 1970; 18: 435–446
  • Carrell R. W., Lehmann H., Lorkin P. A., Raik E., Hunter E. Haemoglobin Sydney: β 67 (El 1) Valine→Alanine: An emerging pattern of unstable haemoglobins. Nature 1967; 215: 626–628
  • Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T. Hemoglobin Mizuho or beta 68 (E12) Leucine→Proline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin 1977; 1: 467–477
  • Salomon H., Tatarski I., Dance N., Huehns E. R., Shooter E. M. A new hemoglobin variant found in a Beduin tribe: Hemoglobin “Rambam”. Israel J. Med. Sci. 1965; 1: 836–840
  • Kurachi S., Hermodson M., Hornung S., Stamatoyannopoulos G. Structure of Haemoglobin Seattle. Nature New Biol. 1973; 243: 275–276
  • Carrell R. W., Owen M. C. A new approach to haemoglobin variant identification. Haemoglobin Christchurch 071 (E15) Phenylalanine→Serine. Biochim. Biophys. Acta 1971; 236: 507–511
  • Jones R. T., Brimhall B., Pootrakul S., Gray G. Hemoglobin Vancouver [â202 73 (E17) Asp→Tyr]: Its structure and function. J. Mol. Evol. 1976; 9: 37–44
  • Konotey-Ahulu F. I. D., Gallo E., Lehmann H., Ringelhann B. Haemoglobin Korle-Bu (β 73 Aspartic acid→Asparagine) showing one of the two amino acid substitutions of Haemoglobin C Harlem. J. Med. Genet. 1968; 5: 107–111
  • Bio-Doku F. S., Kinderlerer J., Lehmann H. Atlas of Protein Sequence and Structure 1972; 5: 73
  • Schneider R. G., Hosty T. S., Tomlin G., Atkins R., Brimhall B., Jones R. T. Hb Mobile [â2β 2 73 (E17) Asp→Val]: A new variant. Biochem. Genet. 1975; 13: 411–415
  • Rieder R. F., Wolf D. J., Clegg J. B., Lee S. L. Rapid postsynthetic destruction of unstable Haemoglobin Bushwick. Nature 1975; 254: 725–727
  • White J. M., Brain M. C., Lorkin P. A., Lehmann H., Smith M. Mild “unstable haemoglobin haemolytlc anaemia” caused by Haemoglobin Shepherds Bush (β 74 (El 8) Gly-Asp). Nature 1970; 225: 939–941
  • Hubbard M., Winton E. F., Lindeman J. G., Dessauer P. L., Wilson J. B., Wrightstone R. N., Huisman T.H.J. Hemoglobin Atlanta or â2β 2 75 Leu→Pro (E19): An unstable variant found in several members of a Caucasian family. Biochim. Biophys. Acta 1975; 386: 538–541
  • Romain P. L., Schwartz A. D., Shamsuddin M., Adams J. G., III, Mason R. G., Vida L. N., Honig G. R. Hemoglobin J-Chicago (β 76 (E20) Ala→Asp): A new hemoglobin variant resulting from a substitution of an external residue. Blood 1975; 45: 387–393
  • Rahbar S., Beale D., Isaacs W. A., Lehmann H. Abnormal haemoglobins in Iran. Observation of a new variant -Haemoglobin J Iran (â202 77 His→Arg). Brit. Med. J. 1967; 1: 674–677
  • Blackwell R. Q., Shin T.-B., Wang C.-L., Liu C.-S. Hemoglobin G-Hsi-Tsou: 079 Asp-Gly. Biochim. Biophys. Acta 1972; 257: 49–53
  • 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: β 80 Asn-Lys. Biochim. Biophys. Acta 1969; 188: 59–64
  • 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, Ubell, Hikari, Gifu, and Agenogi. Biochim. Biophys. Acta 1970; 200: 197–202
  • Schneider R. G., Hettig R. A., Bilunos M., Brimhall B. Hemoglobin Baylor [â2β 2 81 (EF5) Leu→Arg] -an unstable mutant with high oxygen affinity. Hemoglobin 1976; 1: 85–96
  • Moo-Penn W. F., Jue D. L., Bechtel K. C., Johnson M. H., Schmidt R. M., McCurdy P. R., Fox J., Bonaventura J., Sullivan B., Bonaventura C. Hemoglobin Providence. A human hemoglobin variant occurring in two forms in vivo. J. Biol. Chem. 1976; 251: 7557–7562
  • 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 β 82. J. Biol. Chem. 1976; 51(2)7563–7571
  • Lorkin P. A., Stephens A. D., Beard M. E. J., Wrigley P. F. M., Adams L., Lehmann H. Haemoglobin Rahere β 882 Lys →Thr): A new high affinity haemoglobin associated with decreased 2,3-dlphosphoglycerate binding and relative polycythaemia. Br. Med. J. 1975; 4: 200–202
  • 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 β 882 [EF6] Lys→Met). Acta Haematol. 1976; 56: 257–275
  • Blackwell R. Q., Liu C.-S., Wang C.-L. Hemoglobin Ta-li: β 83 Gly→Cys. Biochim. Biophys. Acta 1971; 243: 467–474
  • Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos (â2β 2 83 (EF7) Gly→Asp). A new hemoglobin (Hb) variant. Annual Meeting of the American Society of Hematology. Miami 1972, Abstract 168
  • Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos â2β 2 83 (EF7) Gly→Asp: A new hemoglobin variant in double heterozygosity with Hemoglobin S. Blood 1976; 47: 827–832
  • Bradley T. B., Wohl R. C., Murphy S. B., Oski F. A., Bunn H. F. Properties of Hemoglobin Bryn Mawr, β 85 Phe→Ser, a new spontaneous mutation producing an unstable hemoglobin with high oxygen affinity. Annual Meeting of the American Society of Hematology. Miami 1972, Abstract 40
  • De Weinstein B. I., White J. M., Wiltshire B. G., Lehmann H. A new unstable haemoglobin: Hb Buenos Aires, β 85 (Fl) Phe→Ser. Acta Haematol. 1973; 50: 357–363
  • Watson-Williams E. J., Beale D., Irvine D., Lehmann H. A new haemoglobin, D Ibadan (087 Threonine→Lysine), producing no sickle cell Haemoglobin D disease with haemoglobin S. Nature 1965; 205: 1273–1276
  • Hollender A., Lorkin P. A., Lehmann H., Svensson B. New unstable Haemoglobin Borås: 088 (F4) Leucine→Arginine. Nature 1969; 222: 953–955
  • 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-β 88 (F4) Leucine-Proline. J. Med. Genet. 1968; 5: 292–297
  • 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: 135–150
  • Paniker N. V., Kuang-Tzu Davis Lin, Krantz S. B., Flexner J. M., Wasserman B. K., Puett D. Haemoglobin Vanderbilt (â2β 2 89 Ser→Arg): A new haemoglobin with high oxygen affinity and compensatory erythrocytosis. Br. J. Haematol. 1978; 39: 249–258
  • Miyaji R., Suzuki H., Ohba Y., Shibata S. Hemoglobin Agenogi (â202 90 Lys), a slow moving hemoglobin of a Japanese family resembling Hb-E. Clin. Chim. Acta 1966; 14: 624–629
  • Schneider R. G., Satoshi U., Alperine J. B., Brimhall B., Jones R. T. Hemoglobin Sabine, β 91 (F7) Leu→Pro. An unstable variant causing severe anemia with inclusion bodies. N. Engl. J. Med. 1969; 280: 739–745
  • Ahern E., Ahern C, Hilton T., Serjeant G. R., Serjeant B. E., Seakins M., Lang A., Middleton A., Lehmann H. Haemoglobin Caribbean, β 91 (F7) Leu→Arg: A mildly unstable haemoglobin with low oxygen affinity. FEBS Lett. 1976; 69: 99–102
  • 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: 311–329
  • Beuzard Y., Courvalin J.CI., Cohen-Solal M., Garel M. C., Rosa J., Brizard C. P., Gibaud A. Structural studies of Hemoglobin Saint Etienne 092 (F8) His→Gln: A new abnormal hemoglobin with loss of 0 proximal histidine and absence of heme on the β chains. FEBS Lett. 1972; 27: 76–80
  • 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) 0). J. Clin. Invest. 1972; 51: 2380–2387
  • 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: 403–415
  • Finney R., Casey R., Lehmann H., Walker W. Hb Newcastle: (892 (F8) His-Pro. FEBS Lett. 1975; 60: 435–438
  • Clegg J. B., Naughton M. A., Weatherall D. J. An improved method for the characterization of human haemoglobin mutants: Identification of â2β 2 95 Glu, Haemoglobin N (Baltimore). Nature 1965; 07(2)945–947
  • Gottlieb A. J., Robinson E. A., Itano H. A. Primary structure of Hopkins-I haemoglobin. Nature 1967; 14(2)189–190
  • Dobbs N. B., Jr., Simmons J. W., Wilson J. B., Huisman T. H.J. Hemoglobin Jenkins or Hemoglobin N-Baltimore or â2β 2 95 Glu. Biochim. Biophys. Acta 1966; 117: 492–494
  • 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 (β 143 Histidine→Aspartic acid): A newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia. (Personal communication, P. Heller) 7. Clin. Invest. 1969; 48: 525–S35
  • Moo-Penn W. F., Schneider R. G., Andrian S., Das D. K. Hemoglobin Detroit: β 95 (FG2) Lysine→Asparagine. Biochim. Biophys. Acta 1978; 536: 283–288
  • Lorkin P. A., Lehmann H., Fairbanks V. F., Berglund G., Leonhardt T. Two new pathological haemoglobins: Olmsted 0141 (H19) Leu→Arg and Malmo: β 97 (FG4) His-Gln. Biochem. J. 1970; 119: 68–74
  • Taketa F., Huang Y. P., Libnoch J. A., Dessell B. H. Hemoglobin Wood β 97 (FG4) His→Leu: A new high-oxygen affinity hemoglobin associated with familial erythrocytosis. Biochim. Biophys. Acta 1975; 400: 348–353
  • Taketa F., Antholine W. E., Mauk A. G., Libnoch J. A. Nitrosylhemoglobin Wood: Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum. Biochemistry 1975; 14: 3229–3233
  • Carrell R. W., Lehmann H., Hutchison H. E. Haemoglobin Koln (β 98 Valine→Methionine): An unstable protein causing inclusion-body anaemia. Nature 1966; 210: 915–916
  • 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 Koln. Nature New Biol. 1973; 243: 205–207
  • Gordon-Smith E. C., Dacie J. V., Blecher T. E., French E. A., Wiltshire B. G., Lehmann H. Haemoglobin Nottingham, β (FG5) Val-KJly: A new unstable haemoglobin producing severe haemolysis. Prod. Roy. Soc. Med. 1973; 66: 507–508
  • Gacon G., Wajcman H., Labie D. A new unstable hemoglobin mutated in β [FG5) Val-Ala: Hb Djelfa. FEBS Lett. 1975; 58: 238–240
  • 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: 623–632
  • Jones R. T., Osgood E. E., Brimhall B., Koler R. D. Hemoglobin Yakima: I. Clinical and biochemical studies. \. Clin. Invest. 1967; 46: 1840–1847
  • 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 (â202 99 (Gl) Ala): A high oxygen-affinity variant causing familial polycythaemia. Br. J. Haematol. 1977; 35: 177–191
  • 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 (â2Aβ 2 100 Pro→Leu). Hemoglobin variant associated with familial erythrocytosis. J. Clin. Invest. 1973; 52: 2060–2067
  • Jones R. T., Brimhall B., Gray G. Hemoglobin British Columbia [→202 101 (G3) Glu→Lys]: A new variant with high oxygen affinity. Hemoglobin 1976; 1: 171–182
  • 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: 261–169
  • 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 â2β 02 (101 (G3) Glu→Gly), a new high-oxygen affinity hemoglobin variant causing erythrocytosis. Hemoglobin 1976; 1: 77, 183–194
  • Charache S., Jacobson R., Brimhall B., Murphy E. A., Hathaway P., Winslow R., Jones R., Rath C, Simkovich J. Hb Potomac (β 101 Glu→Asp): Speculations on placental oxygen transport in carriers of high-affinity hemoglobins. Blood 1978; 51: 331–338
  • Efremov G.D, Huisman T. H. J., Smith L. L., Wilson J. B., Kitchens I. L., Wrightstone R. N., Adams H. R. Hemoglobin Richmond, a human hemoglobin which forms asymmetric hybrids with other hemoglobins. J. Biol. Chem. 1969; 44(2)6105–6116
  • Bonaventura J., Riggs A. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. J. Biol. Chem. 1968; 243: 980–991
  • 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: 125–130
  • 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: 665–667
  • Wilkinson T., Ching Geh Chua, Carrell R. W., Robin H., Exner T., Kit Ming Lee, Kronenberg H. A new haemoglobin variant, Haemoglobin Camperdown β 104 (G6) Arginine→Serine. Biochim. Biophys. Acta 1975; 393: 195–200
  • Ryrie D. R., Plowman D., Lehmann H. Haemoglobin Sherwood Forest →104 (G6) Arg -Thr. FEBSLett. 1977; 83: 260–262
  • Hyde R. D., Hall M. D., Wiltshire B. G., Lehmann H. Haemoglobin Southampton, β106 (G8) Leu→Pro: An unstable variant producing severe haemolysis. Lancet 1972; 2: 1170–1172
  • Koler R. D., Jones R. T., Bigley R. H., Litt M., Lovrien E., Brooks R., Lahey M. E., Fowler R. Hemoglobin Casper: β 106 (G8) Leu→Pro, a contemporary mutation. Am. J. Med. 1973; 55: 549–558
  • Kleihauer E., Waller H. D., Benohr H. Chr., Kohne E., Gelinsky P. Hb Tubingen. Eine neue β -Kettenvariante (β Tp 10-12) mit erhohter Spontanoxydation. Klin. Wochenschr. 1971; 48: 651–658
  • Kohne E., Kley P. H., Kleihauer E., Versmold H., Benohr H. C., Braunitzer G. Structural and functional characteristics of the Hb Tubingen: β 106 (G8) Leu→Gln. FEBS Lett. 1976; 64: 443–447
  • Turner J. W., Jr., Jones R. T., Brimhall B., Du Val M. C., Koler R. D. Characterization of Hemoglobin Burke [0107 (G9) Gly→Arg]. Biochem. Gen. 1976; 14: 577–585
  • 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: 2341–2348
  • 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. FEBSLett. 1978; 92: 53–56
  • Nute P. E., Stamatoyannopoulos G., Hermodson M. A., Roth D., Hornung S. Hemoglobinopathic erythrocytosis due to a new electrophoretically silent variant, Hemoglobin San Diego (β 109 (Gil) Val-Mef). J. Clin. Invest. 1974; 53: 320–328
  • King M. A. R, Wiltshire B. G., Lehmann H., Morimoto H. An unstable haemoglobin with reduced oxygen affinity: Haemoglobin Peterborough, β 111 (G13) Valine→Phenylalanine, its interaction with normal haemoglobin and with Haemoglobin Lepore. Br. J. Haematol 1972; 22: 125–134
  • Adams J. G., Boxer L. A., Baehner R. L., Forget B. G., Tsistrokis G. A., Steinberg M. H. Hemoglobin Indianapolis (β 112 [G14] Arginine): An unstable β -chain variant producing the phenotype of severe \3-thalassemia. J. Clin. Invest. 1979; 63: 931–938
  • Ranney H. M., Jacobs A. S., Nagel R. L. Haemoglobin New York. Nature 1967; 213: 876–878
  • Outeirino J., Casey R., White J. M., Lehmann H. Haemoglobin Madrid, β 115 (G17) Alanine→Proline: An unstable variant associated with haemolytic anaemia. Acta Haematol 1974; 52: 53–60
  • Schneider R. G., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin P (âβ S2 117 Arg): Structure and properties. J. Lab. Clin. Med. 1969; 73: 616–622
  • Schneider R. G., Berkman N. L., Brimhall B., Jones R. T. Hemoglobin Fannin-Lubbock [âβ 119 (GIG) Gly→Asp]. A slightly unstable mutant. Biochim. Biophys. Acta 1976; 543: 478–483
  • 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 [âβ2119 (GH2) Gly→Aspj: A new hemoglobin variant at the âlβl contact. Biochim. Biophys. Acta 1976; 453: 472–477
  • Chen-Marotel J., Braconnier F., Blouquit Y., Martin-Caburi J., Kammerer J., Rosa J. Hemoglobin Bougardirey-Mali β 119 (GH2) Gly→Val. An electrophoretically silent variant migrating in isoelectrofocusing as Hb F. Hemoglobin 1979; 3: 253–262
  • Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Hamilton H. B. Hemoglobin Hijiyama: A new fast-moving hemoglobin in a Japanese family. Science 1968; 159: 204–206
  • El-Hazmi M. A. F., Lehmann H. Hemoglobin Riyadh [âβ 32 120 (GH3) Lys→Asn] -a new variant found in association with a-thalassemia and iron deficiency. Hemoglobin 1976; ii(1)59–74
  • Miyaji T., Ohba Y., Matsuoka M., Kudoh H., Asano M., Yamamoto K., Satoh T. Hemoglobin Karatsu: Beta 120 (GH3) Lysine →Asparagine. An example of Hb Riyadh in Japan. Hemoglobin 1977; 1: 461–466
  • Baglioni C. Abnormal human haemoglobins. VII. Chemical studies on Haemoglobin D. Biochim. Biophys. Acta 1962; 59: 437–449
  • Ozsoylo S. Homozygous Hemoglobin D Punjab. Acta Haematol 1970; 42: 353–359
  • Ramot B., Rotem J., Rahbar S., Jacobs A. S., Uden L., Ranney H. M. Hemoglobin D Punjab in a Bulgarian Jewish family. IsraelJ. Med. Sci. 1969; 5: 1066–1070
  • Smith E. W., Conley C. L. Sickle cell-Hemoglobin D disease. Ann. Intern. Med. 1959; 50: 94–98
  • Wasi P., Pootrakul S., Na-Nakorn S., Beale D., Lehmann H. Haemoglobin D Los Angeles (D Punjab, â2β2 125 Glu→NH2) in a Thai family. Acta Haematol. 1968; 39: 151–158
  • Imamura T., Riggs A. Identification of Hemoglobin Oak Ridge with Hemoglobin D Punjab (Los Angeles). Biochem. Genet. 1972; 7: 127–130
  • Bowman B., Ingram V. M. Abnormal human haemoglobins. VII. the comparison of normal human Haemoglobin D Chicago. Biochim. Biophys. Acta 1961; 53: 569–573
  • Baglioni C, Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229–232
  • Kamel K., Hoerman K., Awny A. Ethnological significance of hemoglobin â2β 2 121 Lys. Am. J. Phys. Anthropol 1970; 26: 107–108
  • Efremov G. D., Duma H., Rudivic R., Rolovic Z., Wilson J. B., Huisman T. H.J. Hemoglobin Beograd or â2β2 121 Glu→Val (GH4). Biochim. Biophys. Acta 1973; 28(3)81–83
  • Clegg J. B., Weatherall D. J., Wong Hock Boon, Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature 1969; 22: 379–380
  • Bursaux E., Blouquit Y., Poyart C, Rosa J., Arous N., Bonn B. Hemoglobin Ty Gard (â2Aβ2124 (H2) Pro→Gln): A stable high O2 affinity variant at the â, β1, contact. FEBSLett. 1978; 88: 155–159
  • Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Takenaka H. Japanese haemoglobin variant. Nature 1968; 217: 89–90
  • Altay C, Altinoz N., Wilson J. B., Bolch K. C., Huisman T. H.J. Hemoglobin Hacettepe or â2β 2 127 (H5) Gln-KJlu. Biochim. Biophys. Acta 1976; 434: 1–3
  • Martinez G., Lima F., Colombo B. Haemoglobin J Guantanamo (â2β 2 128 (H6) Ala→Asp). A new fast unstable haemoglobin found in a Cuban family. Biochim. Biophys. Acta 1977; 491: 1–6
  • Blackwell R. Q., Yang Y.-J., Wang C.-C. Hemoglobin J Taichung: (3129 Ala→Asp. Biochim. Biophys. Acta 1969; 194: 1–5
  • Maniatis A., Bousios T., Nagel R. L., Balazs T., Ueda Y., Bookchin R. M., Maniatis G. M. Hemoglobin Crete β 8129 Ala→Pro): A new high-affinity variant interacting with β °-and →β °-thalassemia. Blood 1979; 54: 54–63
  • Lorkin P. A., Pietschmann H., Braunsteiner H., Lehmann H. Structure of Haemoglobin Wien β 130 (H8) Tyrosine→Aspartic acid: An unstable haemoglobin variant. Acta Haematol. 1974; 51: 351–361
  • Wa De Cohen P. T., Yates A., Bellingham A. J., Huehns E. R. Amino acid substitution on the â1\β 1 intersubunit contact of Haemoglobin Camden β 131 (H9) Gln-Glu. Nature New Biol. 1973; 43(2)467–468
  • Ohba Y., Miyaji T., Matsuoka M., Ueda S., Iuchi I., Shibata S. Hemoglobin Tokuchi: β 131 Glutamine→Glutamic acid, an example of Hb Camden in Japan. Acta Haematol. Jap. 1975; 38: 1–7
  • Brennan S. O., Arnold B., Fleming P., Carrell R. W. A new unstable haemoglobin, β 134 Val-Glu. Proc. New Zealand Med. J. 1977; 85: 398
  • Arends T., Lehmann H., Plowman D., Stathopoulou R. Hemoglobin North Shore-Caracas β 134 (H12) Valine→Glutamic acid. FEBSLett. 1977; 80: 261–265
  • Marti H. R., Winterhalter K. H., Di Iorio E. E., Lorkin P. A., Lehmann H. Hb Altdorf â2β 2 135 (H13) Ala→Pro: A new electrophoretically silent unstable haemoglobin variant from Switzerland. FEBSLett. 1976; 63: 193–196
  • Minnich V., Hill R. J., Khuri P. D., Anderson M. E. Hemoglobin Hope: A beta chain variant. Blood 1965; 25: 830–838
  • Tentori L., Carta Sorcini M., Buccella C. Hemoglobin Abruzzo: Beta 143 (H21) His→Arg. Clin. Chim. Acta 1972; 38: 258–262
  • Bromberg P. A., Alben J. O., Bare G. H., Balcerzak S. P., Jones R. T., Brimhall B., Padilla F. Hemoglobin Little Rock 03143 His→Gln: (H21)). A high oxygen affinity haemoglobin variant with unique properties. Nature New Biol. 1973; 243: 177–179
  • Jensen M., Oski F. A., Nathan D. G., Bunn H. F. Hemoglobin Syracuse (â2β 2 143 (H21) His→Pro), a new high-affinity variant detected by special electrophoretic methods. \. Clin. Invest. 1975; 55: 469–477
  • Zak J. S., Brimhall B., Jones R. T., Kaplan M. E. Hemoglobin Andrew-Minneapolis â2Aβ 2 144 Lys→Asn: A new high-oxygen affinity mutant human hemoglobin. Blood 1974; 44: 543–549
  • Hayashim A., Stamatoyannopoulos G., Yoshida A., Adamson J. Haemoglobin Rainier: β 145 (HC2) Tyrosine-Cysteine and Haemoglobin Bethesda: β 145 (HC2) Tyrosine→Histidine. Nature New Biol. 1971; 30(2)264–267
  • 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 â2β 2 145 Tyr→Asp, a new high-oxygen affinity hemoglobin variant. Biochim. Biophys. Acta 1975; 00(4)343–347
  • Charache S., Brimhall B., Jones R. T. Polycythemia produced by Hemoglobin Osier (0145 (HC2) Tyr→Asp). Johns Hopkins Med. J. 1975; 136: 132–136
  • Gacon G., Wajcman H., Labie D. Structural and functional study of Hb Nancy β 145 (HC2) Tyr→Asp: A high oxygen affinity hemoglobin. FEBSLett. 1975; 56: 39–42
  • Winslow R. M., Swenberg M.-L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin McKees Rocks (â202 145 Tyr→Term): A human “nonsense” mutation leading to a shortened β -chain. J. Clin. Invest. 1976; 57: 772–781
  • Imai K. Oxygen-equilibrium characteristics of abnormal Hemoglobin Hiroshima (â202 143 Asp). Arch. Biochem. Biophys. 1968; 127: 543–547
  • Barem G. H., Bromberg P. A., Alben J. O., Brimhall B., Jones R. T., Mintz S., Rother I. Altered C-terminal salt bridges in Haemoglobin York cause high oxygen affinity. Nature 1976; 259: 155–156
  • 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: 354–364
  • Jones R. T., Brimhall B., Huehns E. R., Barnicot N. A. Hemoglobin Sphakia: A delta chain variant of Hemoglobin Â2 from Crete. Science 1966; 151: 1406–1408
  • Ranney H. M., Jacobs A. S., Ramot B., Bradley T. B., Jr. Hemoglobin NYU, a delta chain variant, â282 12 Lys. J. Clin. Invest. 1969; 48: 2057–2062
  • Ball E. W., Meynell M. J., Beale D., Kynoch P., Lehmann H., Stretton A. O.W. Haemoglobin Â2′: â→2 16 Glycine→Arginine. Nature 1966; 209: 1217–1218
  • Rieder R. F., Clegg J. B., Weiss H. J., Christy N. P., Rabinowitz R. Hemoglobin Â2-Roosevelt: â252 20 Val→Glu. Biochim. Biophys. Acta 1976; 39(4)501–504
  • Jones R. T., Brimhall B., Huisman T. H.J. Structural characterization of two 5chain variants. Hemoglobin A2' (BJ and Hemoglobin Flatbush. J. Biol. Chem. 1967; 42(2)5141–5145
  • Sharma R. S., Harding D. L., Wong S. C., Wilson J. B., Gravely M. E., Huisman T. H.J. A new 5 chain variant Haemoglobin Â2-Melbourne or â→2 43 Glu→Lys (CD2). Biochim. Biophys. Acta 1974; 359: 233–235
  • Alberti R., Tentori L., Marinucci M., Borghesi V. Hb A2-Adria (→51 Pro→Arg (D2)): A new 5-chain variant found in association with \3-thalassemia. Hemoglobin 1978; 2: 171–174
  • Lie-Lnjo L. E., Pribada W., Boerma F. W., Efremov G. D., Wilson J. B., Reynolds C. A., Huisman T. H.J. Hemoglobin ArIndonesia or â2→ 69 (E13) Gly→Arg. Biochim. Biophys. Acta 1971; 229: 335–342
  • Sharma R. S., Williams L., Wilson J. B., Huisman T. H.J. Hemoglobin A2-Coburg or â252 116 Arg→His (G18). Biochim. Biophys. Acta 1975; 393: 379–382
  • De Jong W. W. W., Bernini L. F. Haemoglobin Babinga (5136 Glycine→ Aspartic acid): A new delta chain variant. Nature 1968; 219: 1360–1362
  • Lie-Lnjo L. E., Kamuzora H., Lehmann H. Haemoglobin F Malaysia: â2γ2 1 (NA1) Glycine→Cysteine: 136 Glycine. J. Med. Genet. 1974; 11: 25–30
  • Jenkins G. C., Beale D., Black A. J., Huntsman G. R., Lehmann H. Haemoglobin F Texas I (β γ272 5 Glu→Lys): A variant of Haemoglobin F. Br. J. Haematol. 1967; 13: 252–255
  • Ahem E. J., Wiltshire B. G., Lehmann H. Further characterization of Haemoglobin F. Texas Iγ5 Glutamic acid→Lysine: γ136 Alanine. Biochim. Biophys. Acta 1972; 271: 61–64
  • Larkin I. L. M., Baker T., Lorkin P. A., Lehmann H., Black A. J., Huntsman R. G. Haemoglobin F Texas II (âγ2 6 Glu→Lys). the second of the Haemoglobin F Texas variants. Br. J. Haematol 1968; 14: 233–238
  • 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: 323–327
  • Loukopoulos D., Kaltsoya A., Fessas Ph. On the chemical abnormality of Hb “Alexandra” a fetal hemoglobin variant. Blood 1969; 33: 114–118
  • Brennan S. O., Smith M. B., Carrell R. W. Haemoglobin F Melbourne →γl6 Gly→Arg and Haemoglobin F Carlton γ7l21 Glu→Lys. Biochim. Biophys. Acta 1977; 90(4)452–455
  • Lie-Lnjo L. E., Wiltshire B. G., Lehmann H. Structural identification of Haemoglobin F Kuala Lumpur (âγ2 22 (B4) Asp→Gly: (136 Ala). Biochim. Biophys. Acta 1973; 322: 224–230
  • Ahem E. J., Jones R. T., Brimhall B., Gray R. H. Haemoglobin F Jamaica (âγ1 Lys-Glu: 136 Ala). Br. J. Haematol. 1970; 18: 369–375
  • Ahern E., Holder W., Ahem V., Serjeant G. R., Serjeant B. E., Forbes M., Brimhall B., Jones R. T. Haemoglobin F Victoria Jubilee (âγ80 Asp→Tyr). Biochim. Biophys. Acta 1975; 33: 188–194
  • 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 (A-γ 97His→Arg), a new variant. Br. J. Haematol. 1974; 28: 515–524
  • 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; 23(2)311–313
  • Sacker L. S., Beale D., Black A. J., Huntsman R. G., Lehmann H., Lorkin P. A. Haemoglobin F Hull (γ 121 Glutamic acid→Lysine), homologous with Haemoglobins O and O Indonesia. Br. Med. J. 1967; 3: 531–533
  • Brimhall B., Vedvick T. S., Jones R. T., Ahem E., Palomino E., Ahem V. Haemoglobin F Port Royal (â2→γ 125 Glu Ala). Br. J. Haematol 1973; 27: 313–320
  • 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, â2gγ2130 Tryptophan→Glycine. J. Clin. Pathol. 1975; 28: 317–320
  • Barnabas J., Muller C. J. Haemoglobin Lepore Hollandia. Nature 1962; 94(1)931–932
  • Ostertag W., Smith E. W. Hemoglobin-Lepore Baltimore, a third type of a 50 crossover (→50, β86). Eur. J. Biochem. 1969; 10: 371–376
  • Baglioni C. The fusion of two peptide chains in Hemoglobin Lepore and its interpretation as a genetic deletion. Proc. Natl. Acad. Sci., USA 1962; 48: 1880–1886
  • Ohta Y., Yamaoka K., Sumida I., Yanase T. Hemoglobin Miyada, a β→ fusion peptide (anti-Lepore) type discovered in a Japanese family. Nature New Biol. 1971; 34(2)218–219
  • Lehmann H., Charlesworth D. Observation on Haemoglobin P (Congo type). Biochem. J. 1970; 19(1)43
  • Badr F. M., Lorkin P. A., Lehmann H. Haemoglobin P-Nilotic: containing a 0-5 chain. Nature New Biol. 1973; 242: 107–110
  • Huisman T. H. J., Wrightstone R. N., Wilson J. B., Schroeder W. A., Kendall A. G. Hemoglobin Kenya, the product of fusion of 7 and β polypeptide chains. Arch. Biochem. Biophys. 1972; 153: 850–853
  • Milner P. F., Clegg J. B., Weatherall D. J. Haemoglobin H disease due to a unique hemoglobin variant with an elongated â-chain. Lancet April, 1971; 10: 729–732
  • Weatherall D. J., Clegg J. B. The a-chain-termination mutants and their relation to the a-thalassemias. Phil. Trans. Roy. Soc. 1975; 27(B1)411–455
  • Clegg J. B., Weatherall D. J., Contopolou-Griva I., Caroutsos K., Poungouras P., Tsevrenis H. Haemoglobin Icaria, a new chain-termination mutant which causes â thalassemia. Nature 1974; 251: 245–247
  • De Jong W. W. W., Meera Khan P., Bemini L. F. Hemoglobin Koya Dora: High frequency of a chain termination mutant. Am. J. Hum. Genet. 1975; 27: 81–90
  • Flatz G., Kinderlerer J. L., Kilmartin J. V., Lehmann H. Haemoglobin Tak: A variant with additional residues at the end of the β-chains. Lancet 1971; 10: 732–733
  • Imai K., Lehmann H. The oxygen affinity of Haemoglobin Tak, a variant with an elongated \3 chain. Biochim. Biophys. Acta 1975; 412: 288–294
  • Lehmann H., Casey R., Lang A., Stathopoulou R., Imai K., Chinda S., Vinai P., Flatz G. Haemoglobin Tak: A β -chain elongation. Br. J. Haematol. 1975; 31: 119–131, Suppl
  • Seid-Akhaven M., Winter W. P., Abramson R.K. and Rucknagel, D.L.: Hemoglobin Wayne: A frameshift mutation detected in human hemoglobin alpha chains. Proc. Natl. Acad. Sci., USA 1976; 73: 882–886
  • 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 non-homologous crossover between two normal β chain genes. Proc. Natl. Acad. Sci., USA 1975; 72: 3609–3613
  • Huisman T. H. J., Wilson J. B., Gravely M., Hubbard M. Hemoglobin Grady: the first example of a variant with elongated chains due to an insertion of residues. Proc. Natl. Acad. Sci., USA 1974; 71: 3270–3273
  • 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: 129–133
  • 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 â chain and oxygen equilibrium properties. Biochim. Biophys. Acta 1976; 453: 459–471
  • De Jong W. W. W., Went L. N., Bemini L. F. Haemoglobin Leiden: Deletion of β 6 or 7 glutamic acid. Nature 1968; 220: 788–790
  • Cohen-Solal M., Blouquit Y., Garel M. C., Thillet J., Gaillard L., Creyssel R., Gibaud A., Rosa J. Haemoglobin Lyon b17-18 (A14-15) Lys-VaM)) determination of sequenator analysis. Biochim. Biophys. Acta 1974; 351: 306–316
  • 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: 1024–1027
  • Praxedes H., Lehmann H. Haemoglobin Niteroi-a new unstable variant. Proc. 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: 440–445
  • Wajcman H., Labie D., Schapira G. Two new hemoglobin variants with deletion. Hemoglobin Tours: Thr β 87 (F3) deleted and Hemoglobin St. Antoine: Gly-Leu β 74-75 (E18-19) deleted. Consequences for oxygen affinity and protein stability. Biochim. Biophys. Acta 1973; 295: 495–504
  • Bradley T. B., Wohl R. C., Rieder R. F. Hemoglobin Gun Hill: Deletion of five amino acid residues and impaired heme-globin binding. Science 1967; 157: 1581–1583
  • Lutcher C. L., Huisman T. H.J. Hb-Leslie, an unstable variant due to deletion of Gin β 131, 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 β 131 (H9) occurring in association with β °-thalassemia, Hb-C, and Hb-S. Blood 1976; 47: 99–112
  • 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: 0131 (H9) Glutamine-deleted. Biochem. Biophys. Res. Commun. 1975; 65: 8–15
  • Casey R., Kynoch P. A. M., Lang A., Lehmann H., Nozari G., Shinton N. K. Double heterozygosity for two unstable haemoglobins: Hb Sydney (067 [Ell] Val→Ala) and Hb Coventry (β141 [H19] Leu-Deleted). Br. J. Haematol. 1978; 38: 195–209
  • 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 0-polypeptide chain. J. Biol. Chem. 1967; 42(2)248–255
  • Lang A., Lehmann H., McCurdy P. R., Pierce L. Identification of Haemoglobin C Georgetown. Biochim. Biophys. Acta 1972; 278: 57–61
  • Adams G. J., Heller P. Hemoglobin Arlington Park: a new hemoglobin variant with two amino acid substitutions in the β chain. Hemoglobin 1977; 1: 419–426
  • Blackwell R. Q., Wong Hock Boon, Liu C.-S., Weng M. I. Hemoglobin J Singapore: â78 Asn→Asp: â79 Ala→Gly. Biochim. Biophys. Acta 1972; 278: 482–490
  • Goossens M., Garel M. C., Auvinet J., Basset P., Gomes P. F., Rosa J. Hemoglobin C Ziguinchor â2Aβ 2 6 (A3) Glu→Val 058 (E2) Pro-Arg: the second sickling variant with amino acid substitutions in 2 residues of the 0 polypeptide chain. FEBSLett. 1975; 58: 149–154
  • Moo-Penn W. F., Schmidt R. M., Jue D. L., Bechtel K. C., Wright J. M., Home M. K., Haycraft C. L., Roth E. F., Nagel R. L. Hemoglobin S Travis. A sickling hemoglobin with two amino acid substitutions [β 6 (A3) Glutamic acid→Valine and 0142 (H20) Alanine-Valine]. Eur. J. Biochem. 1977; 77: 561–566
  • Marinucci M., Mavilio F., Massa A., Gabbianelli M., Fontanarosa P. P., Camagna A., Ignesti C, Tentori L. A new abnormal human hemoglobin: Hb Prato (â2 31 (B12) Arg-Ser 0j). Biochem. Biophys. Acta 1979; 578: 534–540
  • Abramov A., Lehmann H., Robb L. Hb Shaare Zedek (5â6 ES Lys→Glu). FEBSLett. 1980; 13(1)235–237
  • Adams J. G., III, Steinberg M. H., Newman M. V., Morrison W. T., Benz E. J., Jr., Iyer R. β -Thalassemia present in cisto a new β -chain structural variant, Hb Vicksburg [β 75 (E19) Leu→0]. Proc. Natl. Acad. Sci., USA 1981; 78: 469–473
  • Wajcman H., Elion J., Boissel J. P., Labie D., Jos J., Girot R. A silent hemoglobin variant: Hemoglobin Necker Enfants-Malades (â20 (Bl) His→Tyr). Hemoglobin 1980; 4: 177–184
  • Tatsis B. Hemoglobin Queens (â34 (B15) Leu→Arg): A new variant at the â1β1\S, 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 (â44 (CD2) Pro→Leu) a new variant with increased oxygen affinity. Biochim. Biophys. Acta 1980; 626: 424–431
  • Szelenyi J. G., Horanyi M., Foldi J., Hudacsek J., Istvan L., Hollan S. R. A new hemoglobin variant in Hungary: Hb Savaria -â49(CE7) Ser→Arg. Hemoglobin 1980; 4: 27–38
  • Nakatsuji T., Miwa S., Ohba Y., Miyaji T., Matsumoto N., Matsuoka I. Hemoglobin Tottori (â59 [E8] Glycine→Valine) a new unstable hemoglobin. Hemoglobin 1981; 5: 427–439
  • 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 LA. A new hemoglobin variant: Hb Dagestan a60 (E9) Lys→Glu. Hemoglobin 1981; 5: 133–138
  • Djoumessi S., Rousseaux J., Descamps J., Goudemand M., Dautrevaux M. Hemoglobin Lille, â2 [74 (EF3) Asp-Ala] β2. Hemoglobin 1981; 5: 475–479
  • 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, a75 (EF4) Asp→Ala, a new variant found in China. Hemoglobin 1981; 5: 481–486
  • Iuchi I., Shimasaki S., Hidaka K., Harano T., Ueda S., Shibata S., Mizushima J., Kubo N. Hemoglobin Mizushi (â75 [EF4] Asp→Gly): A new hemoglobin variant observed in a Japanese family. Hemoglobin 1980; 4: 209–214
  • Shibata S., Ueda S., Miyaji T., Imamura T. Hemoglobinopathies in Japan. Hemoglobin 1981; 5: 509–515
  • Benesch R., Personal Communication
  • Ohba Y., Miyaji T., Hattori Y., Fuyuno K., Matsuoka M. Unstable hemoglobins in Japan. Hemoglobin 1980; 4: 307–312
  • Honig G. R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., Kirschmann C. Hemoglobin Petah Tikva (â 110 Ala→Asp): A new unstable variant with â-thalassemia-like expression. Blood 1981; 57: 705–711
  • Schneider R. G., Hightower B., Carpentieri U., Duerst M. L., Shih T. B., Jones R. T. Hemoglobin Oleander â2116 (GH4) Glu→Gln \SJ: Structural and functional characterization. Hemoglobin 1980; 6: 465–480
  • Fleming P. J., Hughes W. G., Farmilo R. K., Wyatt K., Cooper W. N. Hemoglobin Westmead â2122 (H5) His→Gln β 2: A new hemoglobin variant with the substitution in the â,β, contact area. Hemoglobin 1980; 4: 39–52
  • Harano T., Harano K., Ueda S., Shibata S., Iuchi I. Hemoglobin Yusa (β 21 (B3) Asp→Tyr), a new abnormal hemoglobin found in Japan. Hemoglobin 1981; 5: 121–131
  • Moo-Penn W. F., McPhedran P., Bobrow S., Johnson M. H., Jue D. L., Olsen K. W. Hemoglobin Connecticut (β 21 (B3) Asp→Gly): A hemoglobin variant with low oxygen affinity. Amer. J. Hemat. 1981; 11: 137–145
  • Shibata S., Miyaji T., Ohba Y. Abnormal hemoglobins in Japan. Hemoglobin 1980; 4: 395–408
  • Blouquit Y., Braconnier F., Cohen-Solal M., Foldi J., Arous N., Ankri A., Binet J. L., Rosa J. Hemoglobin Pitie-Salpetriere β 34 (B16) Val→Phe a new high oxygen affinity variant associated with familial erythrocytosis. Biochim. Biophys. Acta 1980; 624: 473–478
  • Wilkinson T., Brennan S. O., Carrell R. W., Wells R. M., Como P., Kronenberg H. Hemoglobin Summer Hill (352 (D3) Asp→His a new variant from Sydney, Australia. Hemoglobin 1980; 4: 185–193
  • Marinucci M., Giuliani A., Maffi D., Massa A., Giampaolo A., Mavilio F., Zannotti M., Tentori L. Hemoglobin Bologna (â2β 61 (E5) Lys→Met) an abnormal human hemoglobin with low oxygen affinity. Biochim. Biophys. Acta 1981; 68(6)209–215
  • Brennan S. O., Wells R. M., Smith H., Carrell R. W. Hemoglobin Brisbane: 068 Leu→His. A new high oxygen affinity variant. Hemoglobin 1981; 5: 325–335
  • Johnson C. S., Moyes D., Schroeder W. A., Shelton J. B., Shelton J. R., Beutler E. Hemoglobin Pasadena, âβ2 75 (E19) Leu→Arg: Identification by high performance liquid chromatography of a new unstable variant with Increased oxygen affinity. Biochim. Biophys. Acta 1980; 623: 360–367
  • Johnson M. H., Jue D. L., Patchen L. C., Hartwig E. C., Jr., Schneider N. J., Moo-Penn W. F. Hemoglobin Tampa: β 79 (EF3) Aspartic acid→Tyrosine. Biochim. Biophys. Acta 1980; 623: 119–123
  • Blouquit Y., Braconnier F., Galacteros F., Arous N., Soria J., Zittoun R., Rosa J. Hemoglobin Hotel-Dieu 099 Asp-KJly (Gl). A new abnormal hemoglobin with high oxygen affinity. Hemoglobin 1981; 5: 19–31
  • Iuchi I., Hidaka K., Harano T., Ueda S., Shibata S., Shimasaki S., Mizushima J., Kubo N., Miyake T., Uchida T. Hemoglobin Takamatsu (β 120 (GH3) Lys→Gln): A new abnormal hemoglobin detected in three unrelated families in the Takamatsu area of Shikoku. Hemoglobin 1980; 4: 165–176
  • 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: 347–361
  • Moo-Penn W. F., Schneider R. G., Shih T.-B., Jones R. T., Govindarajan S., Govindarajan P. G., Patchen L. C. Hemoglobin Ohio (β 142 Ala→Asp): A new abnormal hemoglobin with high oxygen affinity and erythrocytosis. Blood 1980; 56: 246–250
  • Hirano M., Ohba Y., Imai K., Ino T., Morishita Y., Matsui T., Shimizu S., Sumi H., Yamamoto K., Miyaji T. Hb Toyoake: β 142 (H20) Ala→Pro. A new unstable hemoglobin with high oxygen affinity. Blood 1981; 57: 697–704
  • Schneider R. G., Bremner J. E., Brimhall B., Jones R. T., Shih T.-B. Hemoglobin Cowtown β146 HC3 His→Leu). A mutant with high oxygen affinity and erythrocytosis. Amer. J. Gin. Pathol. 1979; 72: 1028–1032
  • Hayashi A., Fujita T., Fujimura M., Titani K. A new abnormal fetal hemoglobin, Hb F M-Osaka (âγ2 63 His→Tyr). Hemoglobin 1980; 4: 447–448
  • Fuyuno K., Torigoe T., Ohba Y., Matsuoka M., Miyaji T. Survey of cord blood hemoglobin in Japan and identification of two new 7 chain variants. Hemoglobin 1981; 5: 139–151
  • Adams J. G., III, Morrison W. T., Steinberg M. H. Hemoglobin Parchman: double crossover within a single human gene. Science 1982; 218: 291–293
  • Honig G. R., Shamsuddin M., Mason R. G., Vida L. N. Hemoglobin Lincoln Park: A 6\3 fusion (anti-Lepore) variant with an amino acid deletion in the Schain-derived segment. Proc. Nat. Acad. Sci., USA 1978; 75: 1475–1479
  • Rahbar S., Winkler K., Louis J., Rea C, Blume K., Beutler E. Hemoglobin Great Lakes (β68 [E12] Leucine→Histidine): A new high-affinity hemoglobin. Blood 1981; 58: 813–817
  • Lee-Potter J. P., Deacon-Smith R. A., Lehmann H., Robb L. Haemoglobin Ferndown (â6 [A4] Aspartic acid-Valine). FEBSLett. 1981; 126: 117–119
  • Zeng Y.-T., Huang S.-Z., Liang X., Long G.-F., Lam H., Wilson J. B., Huisman T. H.J. Hb Wuming or â2 11 (A9) Lys→Gln β2. Hemoglobin 1981; 5: 679–687
  • Liang C., Tao H., Lo H., Huang S., Li R., Wang B. Hemoglobin Shuangfeng (â27 (B8) Glu→Lys): A new unstable hemoglobin variant. Hemoglobin 1981; 5: 691–700
  • Harano T., Harano K., Ueda S., Shibata S., Imai K., Ohba Y., Shinohara T., Horio S., Nishioka K., Shirotani H. Hemoglobin Kawachi [â44 (CE2) Pro→Arg]: A new hemoglobin variant of high oxygen affinity with amino acid substitution at â, β2 contact. Hemoglobin 1982; 6: 43–49
  • Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M. Hb Handa [â90 (FG2) Lys→Met]: Structure and biosynthesis of a new slightly higher oxygen affinity variant. Hemoglobin 1982; 6: 379–389
  • Goossens M., Lee K. Y., Liebhaber S. A., Kan Y. W. Globin structural mutant â125 Leu→Pro is a novel cause of â-thalassaemia. Nature 1982; 296: 864–865
  • Djoumessi S., Rousseaux J., Dautrevaux M. Structural studies of a new hemoglobin: Hb J Lens, 013 (A10) Ala→Asp. FEBSLett. 1981; 136: 145147
  • 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; 70(6)203–206
  • Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., Shinohara T., Hori T., Takayama J. Hemoglobin Miyashiro (023 [B5] Val-Gly) an electrophoretically silent variant discovered by the isopropanol test. Hemoglobin 1981; 5: 653–666
  • Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., Matsumoto N. A new unstable hemoglobin, Hb Yokohama β 31 (B13) Leu→Pro, causing hemolytic anemia. Hemoglobin 1981; 5: 667–678
  • 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: 503–507
  • Spivak V. A., Molchanova T. P., Postnikov Yu.V., Aseeva E. A., Lutsenko I. N., Tokarev Yu.N. A new abnormal hemoglobin: Hb Mozhaisk β 92 (F8) His→Arg. Hemoglobin 1982; 6: 169–181
  • Wajcman H., Aguilar J. L., Bascompte I., Labie D., Poyart C, Bohn B. Structural and functional studies of Hemoglobin Barcelona (â β2Gl)→His). J. Mol. Biol 1982; 156: 185–202
  • Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., Chevrier M., Bordahandy C, Rosa J. Hemoglobin Saint Mandé β102 (G4) Asn→Tyr: A new low oxygen affinity variant. FEBS Lett. 1981; 126: 114–116
  • 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 â2γ2 (5 Glu→Gly; 75 He 136 Gly). Hemoglobin 1981; 5: 565–570
  • Yoshinaka H., Ohba Y., Hattori Y., Matsuoka M., Miyaji T., Fuyuno K. A new γ chain variant, Hb F Kotobuki or Aγ 1 6 (A3) Glu→Gly. Hemoglobin 1982; 6: 37–42
  • Johnson C. S., Schroeder W. A., Shelton J. B., Shelton J. R. The first example of a deletion in the human â chain: Hemoglobin Boyle Heights or â2 6(A4) Asp→β \32. Hemoglobin 1983; 7: 125–140
  • 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 a-chain. Biochim. Biophys. Acta 1982; 701: 45–48
  • 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-Hhreonine at position 75 (E19) of the γ chain. Hum. Genet. 1976; 32: 305–313
  • Webber B. B., Lam H., Wilson J. B., Huisman T. H.J. Hb Albany-GA or â211 (A9) Lys →Asn β2. Hemoglobin 1983; 7: 257–262
  • Honig G. R., Shamsuddin M., Vida L. N., Mompoint M., Bowie L., Jones E., Well S. Hb Evanston (â 14 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 [â16 (A14) Lys→sn]: A new fast-moving hemoglobin variant. Hemoglobin 1982; 6: 629–633
  • 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 â20 His→Gln. FEBS Lett. 1983; 145: 128–130
  • Zeng Y.-T., Huang S.-Z., Zhou X.-D., Qui X.-K., Dong Q.-Y., Li M.-Y., Bai J.-H. Hb Shenyang (â26 (B7) Ala→Glu]: A new unstable variant found in China. Hemoglobin 1982; 6: 625–628
  • Dysert P. A., II, Head C. G., Shih T. B., Jones R. T., Schneider R. G. Hb Dallas â2 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 [â 139 (HC1) Lys→Thr]: A new hemoglobin variant with a slightly increased oxygen affinity. Hemoglobin 1983; 7: 85–90
  • Harano T., Harano K., Ueda S., Shibata S., Imai K., Seki M. Hemoglobin Machida [β 6 (A31 Glu→Gln], a new abnormal hemoglobin discovered in a Japanese family: structure, function and biosynthesis. Hemoglobin 1982; 6: 531–535
  • Moo-Penn W. F., Johnson M. H., McGuffey J. E., Jue D. L., Therrell B. L., Jr. Hemoglobin Rio Grande [β 8 (AS) Lys→Thr], a new variant found in a Mexican-American family. Hemoglobin 1983; 7: 91–95
  • Elion J., Wajcman H., Belkhodja-Dunda O., Lapoumeroulie C, Labie D., Messerschmitt J., Staal A. M., Desableno B. Hemoglobin J Amiens, Beta 17 (A14) Lys replaced by Asn. Coincidence of a functionally silent new abnormal hemoglobin and a polycythemia vera. Nouv. Rev. Fr. Hematol 1979; 21: 347–352
  • Brennan S. O., Williamson D., Whisson M. E., Carrell R. W. Hemoglobin Palmerston North β 23 (B5) Val→Phe. A new variant identified in a patient with polycythemia. Hemoglobin 1982; 6: 569–575
  • Arous N., Galacteros F., Fessas Ph., Loukopoulos D., Blouquit Y., Komis G., Sellaye M., Boussiou M., Rosa J. Structural study of hemoglobin Knossos, 027 (B9) Ala→Ser. A new abnormal hemoglobin present as a silent 0-thalassemia. FEBS Lett. 1982; 147: 247–250
  • Boissel J. P., Wajcman H., Labie D., Fabritius H., Cabannes R. Hb J Daloa [β 57 (El) Asn →Asp]: A new variant found in Ivory Coast. Hemoglobin 1982; 6: 433–437
  • Como P. F., Kennett D., Wilkinson T., Kronenberg H. A new hemoglobin with high oxygen affinity Hemoglobin Bunbury: âβ2 [94 (FG1) Asp→Asn]. Hemoglobin 1983; 7: 413–421
  • Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., Miyaji T. Hemoglobin Saitama or 0117 (G19) His→Pro, a new variant causing hemolytic disease. Hemoglobin 1983; 7: 47–56
  • 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 [0120 (GH3) Lys→Ile]: A new fast-moving variant found in China. Hemoglobin 1983; 7: 321–326
  • Kamel K., El-Najjar A., Webber B. B., Chen S. S., Wilson J. B., Kutlar A., Huisman T. H.J. Hb Doha or âβ2 [X-N-Met-l(NAl)Val→Glu]; a new β chain abnormal hemoglobin observed in a Qatari female. Biochim. Biophys. Acta 1985; 831: 257–260
  • Salkie M. L., Gordon P. A., Rigal W. M., Lam H., Wilson J. B., Headlee M. E., Huisman T. H.J. Hb Â2-Canada or â2→2 99 (Gl) Asp→Asn, a newly discovered delta chain variant with increased oxygen affinity occurring in cis to thalassemia. Hemoglobin 1982; 6: 223–231
  • Juricic D., Crepinko I., Efremov G. D., Lam H., Webber B. B., Headlee M. G., Huisman T. H.J. Hb Â2 Zagreb or â2→2 125 (H3) Gln→Glu in association with âβ -thalassemia in a Yugoslavian female. Hemoglobin 1983; 7: 443–448
  • 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 lie: 136 Ala]. Hemoglobin 1982; 6: 397–401
  • Nakatsuji T., Headlee M., Lam H., Wilson J. B., Huisman T. H.J. Hb F-Bonaire-Ga or â2Aβ2 39 (C5) Gln→Arg, characterized by high pressure liquid chromatographic and microsequencing procedures. Hemoglobin 1982; 6: 599–606
  • Honig G. R., Koshy M., Schroeder W. A., Shelton J. B., Shelton J. R. Hemoglobin F Lodz (Gγ1 44 Ser→Arg) a newly identified variant from an American infant of Polish descent. Biochim. Biophys. Acta 1982; 707: 213–216
  • Serjeant G. R., Serjeant B. E., Lehmann H., Dukes M., Robb L. Hb F Kingston [gγ 55 (D6) Met-Arg]. FEBSLett. 1982; 150: 77–80
  • Nakatsuji T., Lam H., Huisman T. H.J. Hb F-Kennestone or â2gγ2 (EF1) 77 His→Arg observed in a Caucasian baby. Hemoglobin 1983; 7: 267–270
  • Nakatsuji T., Lam H., Carver J., Huisman T. H.J. Hb F-Marietta or âγl 80 [EF4] Asp→Asn, observed in a Caucasian baby. Hemoglobin 1982; 6: 407–411
  • Nakatsuji T., Lam H., Wilson J. B., Webber B. B., Huisman T. H.J. Hb F-Columbus-Ga or âγ7 94 (FG1) Asp→Asn. Hemoglobin 1982; 6: 593–598
  • Shelton J. B., Shelton J. R., Espinueva Z., Huynh V., Schroeder W. A., Powars D. Hemoglobin F-Caltech: â gγ120 Lys→Gln. Hemoglobin 1982; 6: 577–592
  • Care A., Marimicci M., Massa A., Maffi D, Sposi N. M., Improta T., Tentori L. Hb F-Siena [â2Aγ2 121 (GH4) Gly→Lys]. A new fetal hemoglobin variant. Hemoglobin 1983; 7: 79–83
  • Honig G. R. 1982, Personal Communication
  • Bradley T. B. 1982, Personal Communication
  • 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 A. J. Mol. Biol 1975; 94: 305–310
  • 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 achain. Biochim. Biophys. Acta 1983; 744: 119–120
  • 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: 65–69
  • Clegg J. B., Weatherall D. J., Milner P. F. Haemoglobin Constant Spring -a chain termination mutant?. Nature 1971; 234: 337–340
  • 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: 860–862
  • Harano T., Harano K., Shibata S., Ueda S., Mori H., Arimasa N. Hemoglobin Okayama [β2 (NÂ2) His-KJln]: a new 'silent' hemoglobin variant with substituted amino acid residue at the 2,3 diphosphoglycerate binding site. FEBS Lett. 1983; 156: 20–22
  • Wilkinson T., Gough P., Owen M. C., Carrell R. W., Kronenberg H. Detection of variants of haemoglobin D in Australia: Haemoglobin D Camperdown â202121 Glu→Val and Haemoglobin D Punjab âβ2 121 Glu→Gln. Med. J. Aust. 1974; 2: 636–637
  • Blackwell R. Q., Liu C.-S., Wang C.-L. Hemoglobin New York in Chinese subjects in Taiwan. Am. J. Phys. Anthropol 1971; 34: 329–334
  • Wajcman H., Jones R. T. Proprietes fonctionelles des hemoglobins humaines mutees en position \373. LNSERM 1977; 70: 269–276
  • Shimasaki S., Iuchi I., Hidaka K., Mizuta W. The survey of abnormal hemoglobin in Kobe district. Jap. J. Hum. Genet. 1983; 28: 127–128
  • Marinucci M., Boissel J. P., Massa A., Wajcman H., Tentori L., Labie D. Hemoglobin Maputo: a new β -chain variant (âβ 2 47 (CD6) Asp→Tyr) in combination with Hb S, identified by high performance liquid chromatography (HPLC). Hemoglobin 1983; 7: 423–433
  • Harano T., Harano K., Shibata S., Ueda S., Imai K., Tsuneshige A., Yamada H., Seki M., Fukui H. Hemoglobin Kariya [â40 (C5) Lys→Glu] a new hemoglobin variant with an increased oxygen affinity. FEBS Lett. 1983; 153: 332–334
  • 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: 365–370
  • Como P. F., Barber S., Sage R. E., Trent R. J., Kronenberg H. Hemoglobin Woodville: â6 (A4) Aspartic Acid→Tyrosine. Hemoglobin 1986; 10: 135–141
  • 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 â-chain. Biochim. Biophys. Acta 1982; 01(7)45–48
  • Nakatsuji T., Wilson J. B., Huisman T. H.J. Hb Cordele â2 47 (CE5) Asp→Ala β2 a mildly unstable variant observed in Black twins. Hemoglobin 1984; 8: 37–46
  • 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 (â-78 Asn→Asp), a newly discovered hemoglobin variant with the same amino acid substitution as one of the two present in Hb J-Singapore (â-78 Asn→Asp, â-79 Ala→Gly). Biochim. Biophys. Acta 1984; 784: 187–188
  • 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 â2 102 (G9) Ser→Arg & and Hemoglobin Contaldo or â2 103 (G10) His→Arg β2 by high performance liquid chromatography. Hemoglobin 1984; 8: 169–181
  • 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 (88 (A5) Lys→Gln. Chinese Hematol. J. 1982; 3: 263–265
  • Wong S. C., Ali M. A. M., Lam H., Webber B. B., Wilson J. B., Huisman T. H.J. Hemoglobin Hamilton or β 11 (A8) Val→Ile, a silent β -chain variant detected by Triton X-100 acid-urea polyacrylamide gel electrophoresis. Am. J. Hematol. 1984; 16: 47–52
  • Williamson D., Brennan S. O., Muir H., Carrell R. W. Hemoglobin Collingwood β360 (E4) Val→Ala -a new unstable hemoglobin. Hemoglobin 1983; 7: 511–519
  • 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, (878 (EF2) Leu -Arg, a new abnormal hemoglobin found in Guangdong, China. Hemoglobin 1983; 7: 407–412
  • Hedlund B., Paine S., Smith CM. N., 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: 75–78
  • Brennan S. O., Williamson D., Smith M. B., Cauchi M. N., Macphee A., Carrell R. W. Hb Â2 Victoria 524 (B6) Gly→Asp, a new → chain variant occurring with 0-thalassemia. Hemoglobin 1984; 8: 163–168
  • Garcia C. R., Navarro J. L., Lam H., Webber B. B., Headlee M. G., Wilson J. B., Huisman T. H.J. Hb Â2-Manzanares or â→2 121 (GH4) Glu→Val, an unstable → chain variant observed in a Spanish family. Hemoglobin 1983; 7: 435–442
  • Nakatsuji T., Lam H., Huisman T. H.J. Hb F-Calluna or â→2 (12 Thr→Arg; 75 He; 136 Ala) in a Caucasian baby. Hemoglobin 1983; 7: 563–566
  • Zeng T. Y., Huang S. Z., Nakatsuji T., Huisman T. H.J. -Gγ-Thalassemia and 7-chain variants in Chinese newborn babies. Am. J. Hematol 1985; 18: 235–242
  • Nakatsuji T., Shimizu K., Huisman T. H.J. Hb F-La Grange or âγ2 101 (G3) Glu→Lys; 75 He; 136 Gly; a high oxygen affinity fetal hemoglobin variant observed in a Caucasian newborn. Biochim. Biophys. Acta 1984; 789: 224–228
  • 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: 426–432
  • Moo-Penn W. F., Baine R. M., Jue D. L., Johnson M. H., McGuffey J. E., Benson J. M. Hemoglobin Evanston: â14 (A12) Trp→Arg, a variant hemoglobin associated with a-thalassemia-2. Biochim. Biophys. Acta 1983; 747: 65–70
  • 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-K31y, 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 âβ contact: Hb Chemilly âβ2 99 (Gl) Asp→Val. FEBS Lett. 1984; 166: 8–12
  • 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 (â2β2 140 (H18) Ala→Thr): A new high oxygen-affinity variant with altered bisphosphoglycerate binding. Biochim. Biophys. Acta 1984; 785: 14–21
  • Harano T., Harano K., Shibata S., Ueda S., Mori H., Seki M. Hemoglobin Aichi [â50 (CE8) His→Arg]: A new slightly unstable hemoglobin variant discovered in Japan. FEBS Lett. 1984; 169: 297–299
  • Chih-Chuan L., Fei X., Kegong Y., Song-Sen C, Peichen J., Maoqi Z., Zhiheng Z. Hemoglobin GuiZhou or â 77 (EF6) PRO-ÅG β2, a new slow-moving hemoglobin variant observed in China. Hemoglobin 1984; 2: 387–390
  • 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 (â2 (NÂ2) Leu →Arg) and Hemoglobin Harbin (âl6 (A14) Lys-Met) found in China. Hemoglobin 1984; 8: 569–581
  • Houjun L., Dexiang L., Zhiguo L., Ping L., Ly L., Ji C, Shaozhi H. A new fast-moving hemoglobin variant, Hb J-Tashikuergan â19 (AB1) Ala→Glu. Hemoglobin 1984; 8: 391–395
  • Jeppsson J. O., Kallman L., Lindgren G., Fagerstam L. G. Hb Linkoping (β 36 Pro→Thr): a new hemoglobin mutant characterized by reversed-phase high performance liquid chromatography. J. Chromatog. 1984; 297: 31–36
  • Blouquit Y., Delanoe-Garin J., Lacombe C, Arous N., Cayre Y., Peduzzi J., Braconnier F., Galacteros F. Structural study of hemoglobin Hazebrouck, (338 (C4) Thr→Pro: A new abnormal hemoglobin with instability and low oxygen affinity (FEBS 1563). FEBSLett. 1984; 172: 155–158
  • Rahbar S., Asmerom Y., Blume K. G. A silent hemoglobin variant detected by HPLC: Hemoglobin City of Hope β 69 (E13) GLY-ßR. Hemoglobin 1984; 8: 333–342
  • Williamson D., Brennan S. O., Strosberg H., Whitty J., Carell R. W. Hemoglobin Â2 Fitzroy 5142 ALA→ASP: A new Delta-Chain variant. Hemoglobin 1984; 8: 325–332
  • Moo-Penn W. F., Johnson M. H., McGuffey J. E., Jue D. L. Hemoglobin Shelby [β 131 (H9) GLN→LYS]: A correction to the structure of Hemoglobin Deaconess and Hemoglobin Leslie. Hemoglobin 1984; 8: 583–593
  • Harano K., Harano T., Shibata S., Ueda S., Mori H., Seki M. Hb Okazaki β 93 (F8) Cys→Arg], a new hemoglobin variant with increased oxygen affinity and instability. FEBSLett. 1984; 173: 45–47
  • Jones R. T., Head C, Shih M. F.-C., Shih D. T.-B, Dana B., Jones M. B., Koler R. D. Hemoglobin Linkoping [036 (C2) Pro→Thr] in a large Finnish family from Astoria, Oregon, USA. Hemoglobin 1986; 10: 455–467
  • 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 Aires, Argentina 1984
  • Delano J., North M. L., Arous N., Bardakdjian J., Pflumio F., Brunagel M. L., Lacombe C, Poyart C, Galacteros F., Rosa J., Blouquit Y. Hb Saverne: a new variant having an elongated β chain. Blood 1984; 64: 56a, Suppl. 1
  • Wilson C. I. D., Cave R. J., Lehmann H., Close M., Imai K. Haemoglobin Warwickshire (β 5 [Â2] Pro→Arg): A possible 'fine tuning' of 2,3-DPG affinity by 05 Pro (FEBS 1918). FEBSLett. 1984; 76(1)331–333
  • Guis M., Mentzer W. C., Jue D. L., Johnson M. H., McGuffey J. E., Moo-Penn W. F. Hemoglobin Twin Peaks â113 (GH1) Leu→His. Hemoglobin 1985; 9: 175–177
  • Chen S. S., Webber B. B., Wilson J. B., Huisman T. H.J. Hb Gainesville-GA or âβ2 46 (CD5) Gly-Arg. Hemoglobin 1985; 9: 179–181
  • Delanoe-Garin J., Arous N., Blouquit Y., Hafsia R., Bardakdjian J., Lacombe C, Rosa J., Galacteros F. Hemoglobin Kenitra âβ2 69 (E13) Gly→Arg. A new β variant of elevated expression associated with a-thalassemia, found in a Moroccan woman. Hemoglobin 1985; 9: 1–9
  • Devaraj R., Wilson J. B., Huisman T. H.J. Hb Regina or â1β2 96 (FG3) Leu→Val, a high oxygen affinity variant discovered by cation-exchange HPLC. Am. J. Hematol 1985; 19: 195–200
  • 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 β 97 (FG4) His-Pro. Hemoglobin 1985; 9: 11–24
  • Wilson J. B., Webber B. B., Huisman T. H.J. Annotation: Hb Leslie is the same as Hb Shelby or âβ 131 (H9) Gln→Lys. Hemoglobin 1984; 8: 595–596
  • Chen S. S., Wilson J. B., Webber B. B., Huisman T. H. J., Miwa S., Amenomori Y. Hb F-Tokyo or â2γ2 34 (B16) VaMle, a silent γ chain variant detected by reverse phase high performance liquid chromatography. Hemoglobin 1985; 9: 25–32
  • Chen S. S., Wilson J. B., Huisman T. H.J. Hb F-Pendergrass, and V variant with a Pro→Arg substitution at position âγ36 (C2). Hemoglobin 1985; 9: 73–77
  • 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 â2Aγ2 79 (EF3) Asp→Asn. Hemoglobin 1985; 9: 171–173
  • Blouquit Y., Lena-Russo D., Delanoe J., Arous N., Bardakdjian J., Lacombe C, Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille âβ2 1 (Al) NH2-Met, 2 (Â2) 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 [â141 (HC3) Arg→Cys]. Notable influence of the carboxy-terminal cysteine upon various physico-chemical characteristics of hemoglobin. J. Clin. Invest. 1985; 75: 695–701
  • 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 a Pitre âβ2 90 (F6) Glu→Gly: a new hemoglobin variant with slight instability and low oxygen affinity. FEBS Lett. 1985; 184: 10–13
  • 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 ofN.S.W. Thalassemia Society, 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: 4602–4605
  • Blouquit Y., Arous N., Lena D., Delanoe-Garin J., Lacombe C, Bardakdjian J., Vovan L., Orsini A., Rosa J., Galacteros F. Hb Marseille [â2β N methionyl-2 (NA2 His→Pro]: a new β chain variant having an extended N-terminus. FEBS Lett. 1984; 178: 315–318
  • Shelton J. B., Shelton J. R., Schroeder W. A., Powars D. R. Hb Aztec or â276 (EF5) Met→Thrβ2 detection of a silent mutant by high performance liquid chromatography. Hemoglobin 1985; 9: 325–332
  • Harano T., Harano K., Ueda S. Hb Owari [â121 (H4) Val→Met]: a new hemoglobin variant with a neutral-to-neutral amino acid substitution detected by isoelectric focusing. Hemoglobin 1986; 10: 127–134
  • 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 â2 136 (H19) Leu→Met β2. Hemoglobin 1986; 10: 495–505
  • Rahbar S., Louis J., Lee T., Asmerom Y. Hemoglobin North Chicago (β 36 [C2] Proline→Serine): A new high affinity hemoglobin. Hemoglobin 1985; 9: 559–576
  • 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 â2-β2 65 (E9) Lys→Met in a Turkish family and Hb Complutense or âβ2 127 (H5) Gln→Glu in a Spanish family; correction of a previously published identification. Biochim. Biophys. Acta 1986; 871: 229–231
  • Harano T., Harano K., Ueda S., Imai N., Kitazumi T. A new electrophoretically-silent hemoglobin variant: Hemoglobin Kofu or â2β2 84 (EF8) Thr-Ile. Hemoglobin 1986; 10: 417–420
  • 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 β 140 (H18) Ala→Asp, a slightly unstable hemoglobin with increased N-terminal glycation. Hemoglobin 1986; 10: 109–125
  • Harano K., Harano T., Ueda S., Ohkushi T., Imai K. A new hemoglobin variant, Hb Mito β 144 (HC1) Lys→Glu], with increased oxygen affinity. FEBS Lett. 1985; 192: 75–78
  • Ohba Y., Igarashi M., Tsukahara M., Nakashima M., Sanada C, Ami M., Arai Y., Miyaji T. Hb A Yokoshima, â→25 (B7) Gly→Asp, a new → chain variant found in a Japanese Family. Hemoglobin 1985; 9: 613–615
  • Fujita S., Ohta Y., Saito S., Kobayashi Y., Naritomi Y., Kawaguchi T., Imamura T., Wada Y., Hayashi A. Hemoglobin Â2 Honai (â→90 (F6) Glu→Val): A new delta chain variant. Hemoglobin 1985; 9: 597–607
  • 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: 15–20
  • Chen S-S., Webber B. B., Kutlar A., Wilson J. B., Huisman T. H.J. Hb F-Cobb or â2Aγ237 (C3) Trp→Gly. Hemoglobin 1985; 9: 617–619
  • Chen S-S., Wilson J. B., Webber B. B., Huisman T. H.J. Hb F-Beech Island or â2Aγ253 (D4) Ala→Asp. Hemoglobin 1985; 9: 525–529
  • Boissel J-P., Kasper J. T., Shah S.C, Malone J.L, Bunn H. F. Amino-terminal processing of proteins: Hemoglobin South Florida, a variant with retention of initiator methionine and N.,-acetylation. Proc. Natl. Acad. Sci., USA 1985; 82: 8448–8452
  • Barwick R. C., Head C. G., Shih M.F-C, Block S. H., Jones R. T. Hb T-Cambodia [Beta 26 (B8) Glu→Lys, Beta 121 (GH4) Glu→Gln]: a new doubly substituted beta globin variant found in a Cambodian family. Blood 1985; 66: 68a, Suppl. 1
  • 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: 192–196
  • 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 Lβ32 56 (D7) Gly→Arg and 86 (F2) Ala-Pro. Eur. J. Biochem. 1985; 153: 655–662
  • Como P. F., Raven J. L., Wilkinson T., Kronenberg H. Comparison of the six hemoglobin variants occurring at the â6 (A4) position with particular reference to the a6 Asp→Gly substitution found in Perth, Western Australia. Haematology Society of Australia. PerthWestern Australia October, 1984
  • Chen S. S., Webber B. B., Wilson J. B., Huisman T. H.J. Hb F-Forest Park, a new AgM 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: 242–247
  • 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: 196–202
  • Monplaisir N., Merault G., Poyart C, Rhoda M. D., Craescu C. T., Vidaud M., Galacteros F., Blouquit Y., Rosa J. Hb S Antilles (âβ2j82 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: 9363–9367
  • 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 l-chain. Hemoglobin 1986; 10: 469–481
  • Baiget M., Gomez Pereira C, Jue D. L., Johnson M. H., McGuffey J. E., Moo-Penn W. F. A case of Hemoglobin Indianapolis [j3112(G14) Cys→Arg] in an individual from Cordoba, Spain. Hemoglobin 1986; 10: 483–494
  • De Pablos J. M. A., Wilson J. B., Kutlar A., Chen S. S., Huisman T. H.J. Hb F-Albaicin or g-γ8(AS)Lys-Glu or Gin. Hemoglobin 1986; 10: 655–659
  • Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Gonzalez Redondo J. M., Huisman T. H.J. Hb F-Clarke or â2gγ265(E9)Lys→Asn. Hemoglobin 1987; 11: 185–188
  • Kleman K., Lubin B., Wilson J. B., Kutlar A., Webber B. B., Huisman T.HJ. Hb F-Oakland or â2gγ226(B8)Glu-Lys. Hemoglobin 1987; 11: 181–183
  • Indrak K., Wiedermann B. F., Batek F., Wilson J. B., Webber B. B., Kutlar A., Huisman T.HJ. Hb Olomouc or âβ2 86(F2)Ala-Asp, a new high oxygen affinity variant. Hemoglobin 1987; 11: 151–155
  • Jen P. C., Liu Y. Hemoglobin Guangzhou, â64(E13)Asp→Gly, a new abnormal hemoglobin found in Guangzhou, China. Hemoglobin 1987; 11: 23–30
  • Zhou Z-q., Chen L-c, Chen P-f., Zhang K-Q., Wang Y-H. Hemoglobin Hangzhou, âE13)Asp→Gly, a new variant found in China. Hemoglobin 1987; 11: 31–33
  • Ohba Y., Yamamoto K., Kawata R., Miyaji T., Hyperunstable Hemoglobin Toyama â2136 (H19) Leu→Arg β2 detection and identification by in vitro biosynthesis
  • Merault G., Keclard L., Garin J., Poyart C, Blouquit Y., Arous N., Galacteros F., Feingold J., Rosa J. Hemoglobin La Desirade â2β2 129 (H7) Ala→Val: A new unstable hemoglobin. Hemoglobin 1986; 10: 593–605
  • Fleming P. J., Sumner D. R., Wyatt K., Hughes W.G, Melrose W. D., Jupe D. M. D., Baikie M. J. Hemoglobin Hobart or â20(Bl)His→Arg: A new â chain hemoglobin variant. Hemoglobin 1987; 11: 211–220
  • Williamson D., Wells R. M. G, Anderson R., Matthews J. A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [β 25(B7) Gly→Asp]. Hemoglobin 1987; 11: 221–230
  • Masala B., Manca L., Stangoni A., Cuccuru G. B., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Sassari or â2126 (H9)Asp→Hisβ2 observed in a family from Northern Sardinia. Hemoglobin 1987; 11: 373–378
  • 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: 453–464
  • Hu H., Ma M. Hb F-Xinjiang or AγT25(B7)Gly→Arg: a new slow-moving unstable fetal hemoglobin variant. Hemoglobin 1987; 11: 465–472
  • 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: 473–479
  • Como P. F., Hocking D., Trent R. A., Wilkinson T., Wylie B. R., Bruce D., Kronenberg H. Hb Geelong (β 139 Asn→Asp) and Hb Stanmore (β 111 Val→Ala). 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 cisor trans. Book of Abstracts XXI Congr. Internatl. Soc. Haematol, and XIX Congr. Internatl. Soc. 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: 51–53
  • Dahmane-Arbane M., Blouquit Y., Arous N., Bardakdjian J., Benamani M., Riou J., Benabadji M., Rosa J., Galacteros F. Hb Boumerdès â237 (C2)Pro→Aβ 32: a new variant in an a chain associated with Hb S in an Algerian family (in French). Nouv. Rev. Fr. 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 [(327(B9) Ala→Val], a new variant with normal expression and increased affinity for oxygen. FEBS Lett. 1987; 23(2)59–62
  • 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 â2β236(C2)Pro→Thr), characterized by mass spectrometry. Acta Haematol. 1987; 78: 109–113
  • 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 [β 131 (H9)GIn→Pro] found in China. Br. J. Haematol. 1987; 67: 221–223
  • Gilbert A. T., Fleming P. J., Sumner D. R., Hughes W. G., Ip F., Kwan Y. L., Holland R. A. B. Hemoglobin Randwick or β 15(A12) Trp→GIy: A new unstable β -chain hemoglobin variant. Hemoglobin. 1988; 12: 149–161
  • Mrad A., Blouquit Y., Lacombe C, Blibech R., Arous N., Bardakdjian J., Kastally R., Rosa J., Galacteros F. Hb Tunis: A new β chain variant âβ2(H2)124Pro-Ser, identified by HPLC. Hemoglobin 1988; 12: 23–30
  • De Pablos J. M. A., Kutlar A., Wilson J. B., Webber B. B., Hu H., Huisman T. H.J. Hb D-Granada or âβ222(B4)Glu→Val. Hemoglobin 1987; 11: 563–565
  • 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: 171–177
  • Altay C, Gurgey A., Wilson J. B., Hu H., Webber B. B., Kutlar F., Huisman T. H.J. Hb F-Baskent or â2Aγl28(H6)Ala-Thr. Hemoglobin 1988; 12: 87–89
  • 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 a2β2CCDSJSer-Phe, a mildly unstable hemoglobin variant. Hemoglobin 1988; 12: 163–170
  • Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., Briere J., Galacteros F. Hemoglobin Brest [β 127(H5) Gln→Lys] a new unstable human hemoglobin variant located at the âβ 1 interface with specific electrophoretic behavior. Hemoglobin 1988; 12: 179–188
  • 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 [β 36(C2)Pro→Thr], Hb Caribbean [β 91(F7)Leu→Arg], and Hb Sunnybrook β S36(C2) Pro→Arg]. Hemoglobin 1988; 12: 137–148
  • 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 â2(minus Tyr-Arg) β2, a high oxygen affinity achain variant with a deleted carboxy-terminus resulting from a TAC-T´A (Tyr→terminating codon) mutation in codon a140. Biochim. Biophys. Acta 1988; 951: 36–41
  • Harano T., Harano K., Imai N., Ueda S., Seki M. An electrophoretically silent hemoglobin variant, Hb Hekinan [â27(B8)Glu→Asp] found in a Japanese. Hemoglobin 1988; 12: 61–65
  • 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 â220(Bl)His→Gln\β2 found in a Spanish family. Hemoglobin 1988; 12: 201–205
  • Wajcman H., Blouquit Y., Gombaud-Saintonge G., Riou J., Galacteros F. Hemoglobin Fontainebleau [â21(B2)Ala→Pro], a new silent mutant hemoglobin. Hemoglobin 1989; 13: 421–428
  • Wacjman J., Gombaud-Saintonge G., Galacteros F., Martha M., Vertongen F. Hb Belliard [â56(E5)Lys→Asn] a new fast-moving â chain variant found in a subject of Spanish origin. Hemoglobin 1989; 13: 157–162
  • Gonzalez-Redondo J. M., Wilson J. B., Kutlar A., Huisman T. H. J., Sicilia A., Romero C, Fernandes Fuertes I. Hb J-Pontoise or â263(E12)Ala→Aspβ2 in four members of a Spanish family. Hemoglobin 1987; 11: 47–50
  • Bardakdjian-Michau J., Lacombe C, Blouquit Y., Craescu C. T., Galacteros F., Lena-Russo D., Orsini A., Vovan L. Hemoglobin N-Timone [â2β28(A5)Lys→Glu]: A new fast-moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743–747
  • Gilbert A. T., Fleming PJ., Sumner D. R., Hughes W. G., Holland R. A. B., Tibben E. A. Hemoglobin Windsor or β 11(A8)Val→Asp: A new unstable β -chain hemoglobin variant producing a hemolytic anemia. Hemoglobin 1989; 13: 437–453
  • Gonzalez-Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., Hu H., Wilson J. B., Huisman T. H.J. Hb Monroe or â2β230(B12) Arg→Thr, a variant associated with \3-thalassemia due to a G→C substitution adjacent to the donor splice site of the first intron. Hemoglobin 1989; 13: 67–74
  • Honig G. R., Telfer M. C., Rosenblum B. B., Vida L. N. Hb Warsaw (β 42 Phe→Vai): An unstable hemoglobin with decreased oxygen affinity. I. Hematologic and clinical expression. Am. J. Hematol. 1989; 32: 36–41
  • Bernini L. F., Giordano P. C. Hemoglobin Tilburg: â2-β273 (E17) Asp→Gly. A new hemoglobin with reduced oxygen affinity. Biochim. Biophys. Acta 1988; 57(9)281–285
  • Hidaka K., Iuchi I., Miyake K., Nakahara H., Iwakawa G. Hb Fukuyama [β 77(EFl)His→Tyr]: A new abnormal hemoglobin discovered in a Japanese. Hemoglobin 1988; 12: 391–394
  • 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 [â2Aβ295(FG2) Lys→Met] a new Hb variant found in Argentina. Hemoglobin 1988; 12: 1–11
  • Ohba Y., Imai K., Kumada I., Ohsawa A., Miyaji T. Hb Moriguchi or âβ S297(FG4)His→Tyr substitution at the a,-j82 interface. Hemoglobin 1989; 13: 367–376
  • 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: 1688–1691
  • Blanke S., Johnsen A., Wimberley P. D., Mortensen H. B. Hemoglobin Hafnia: â2(β 116 (G18) His→Gln)2; a new hemoglobin variant mistaken for glycated hemoglobin. Biochim. Biophys. Acta 1988; 55(9)214–219
  • Keclard L., Campier A., Merault G., Auperin A., Riou J., Rosa J., Galacteros F. Hemoglobin Nevers [â2β2130(H8)Try→Ser] a new silent variant found in France. Hemoglobin 1990; 14: 103–107
  • Villegas A., Martin G., Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H.J. Hb Extremadura or â2β2133(Hl 1) Val→Leu, a mildly unstable hemoglobin in a Spanish female. Hemoglobin 1989; 13: 505–508
  • 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 [β 138(H16) Ala→Pro]: An unstable variant near the C-terminus of the β -subunits with normal oxygen-binding properties. Biochemistry 1988; 27: 7614–7619
  • Moo-Penn W. F., Johnson M. H., Jue D. L., Lonser R. Hemoglobin Hinsdale [β 139(H17)Asn→Lys]: A variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate. Hemoglobin 1989; 13: 455–464
  • de Pablos J.Ma, Clegg J. B. Hb F-Granada or â2gγ222(B4)Asp-Val: A new human fetal hemoglobin variant. Hemoglobin 1988; 12: 405–407
  • Kutlar A., Kutlar F., Wilson J. B., Webber B. B., Hu H., Huisman T. H.J. Hb F-Austell or â2g7240(C6)Arg-Lys. Hemoglobin 1988; 12: 409–411
  • Hidaka K., Iuchi I., Nakahara H., Iwakawa C. Hb F-Fukuyama or AγT43(CD2)Asp-Asn. Hemoglobin 1989; 13: 93–96
  • Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H., Orsini A., Rosa J., Galacteros F. Hemoglobin Bruxelles: âβ41 or 42 (C7 or CD1) Phe→deleted. Hemoglobin 1989; 13: 465–474
  • 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)â and Thr-38(C3)â) -Nonallelic gene conversion in the globin system?. J. Biol. Chan. 1989; 264: 21454–21457
  • 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: 311–321
  • 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: 337–352
  • 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: 251–252
  • 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: 443–444
  • Brennan S. O., Williamson D., Symmans W. A., Carrell R. W. Two de novomutations in one β globin chain: Hemoglobin Atlanta-Coventry, β 75 Leu→Pro and 0141 Leu→deleted. Hemoglobin 1986; 10: 225–237
  • Ahmad A., Naqvi S., Ehsanullah S., Zaidi Z. H. Abnormal hemoglobins11 = Hb (Karachi), an â chain abnormality at position 5 Ala→Pro. JPMA 1986; 36: 206–208
  • 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 â223(B4)Glu→Lysβ2 observed in members of a Surinam family in association with a-thalassemia-2 and with Hb S. Hemoglobin 1989; 13: 543–556
  • Bardakdjian-Michau J., Rosa J., Galacteros F., Lancelot M., Marquart F. X. Hb Reims [â223(B4)Glu→Glyβ2]: A new â chain variant with slightly decreased stability. Hemoglobin 1989; 13: 733–735
  • Groff P., Galacteros F., Kalmes G., Blouquit Y., Wajcman H. Hb Luxembourg [â24(B5)Tyr→His]: A new unstable variant. Hemoglobin 1989; 13: 429–436
  • Ohba Y., Imai K., Uenaka R., Ami M., Fujisawa K., Itoh K., Hirakawa K., Miyaji T. Hb Miyano or a41(C6)Thr→Ser: A new high oxygen affinity a chain variant found in an erythremic blood donor. Hemoglobin 1989; 13: 637–647
  • Giordano P. C., Fodde R., Amons R., Ploem J. E., Bernini L. F. Hemoglobin J-Anatolia [â61(E10)Lys→Thr]: Structural characterization and gene localization of a new a chain variant. Hemoglobin 1990; 14: 119–128
  • 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 â262(Ell)Val→Metβ2; an unstable hemoglobin causing a mild hemolytic anemia. Hemoglobin 1989; 13: 557–566
  • 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 [a88(F9)Ala→Ser]. Eur. J. Biochem. 1988; 77(1)307–312
  • Wajcman H., Delaunay J., Francina A., Rosa J., Galacteros F. Hemoglobin Nouakchott [âll4(GH2)Pro→Leu]: A new hemoglobin variant displaying an unusual increase in hydrophobicity. Biochim. Biophys. Acta 1989; 98(9)25–31
  • 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 â2130(H13)Ala→Pro\β2, a new unstable variant occurring in low quantities. Hemoglobin 1990; 14: 479–489
  • 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 subunit assembly properties of Hemoglobin Attleboro [âl38 (H21) Ser→Pro], a variant possessing a site mutation at a critical C-terminal residue. Biochemistry 1990; 29: 173–178
  • Harano T., Harano K., Ueda S., Imai K., Ohkuma A., Koya Y., Takahashi H. Hb Fukuoka [β 2(NÂ2)His→Tyr]: A new abnormal hemoglobin with a substituted amino acid at the 2,3-diphosphoglycerate binding site. Hemoglobin 1990; 14: 199–205
  • 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 thalassemia major. Br. J. Haematol. 1989; 72: 73–80
  • 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: 1041–1045
  • 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 â2β 239 (C5)Gln→Arg, observed in a Chinese family living in Gansu. Hemoglobin 1990; 14: 569–570
  • Honig G. R., Vida L. N., Rosenblum B. B., Perutz M. F., Fermi G. Hemoglobin Warsaw [Pheβ42(CD1)→Val], an unstable variant with decreased oxygen affinity -Characterization of its synthesis, functional properties, and structure. J. Biol. Chem. 1990; 65(2)126–132
  • Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Gainesville-GA or (â2β2 (CDSJGly-Arg; second report. Hemoglobin 1989; 13: 623–624
  • Sciarratta G. V., Ivaldi G. Hb Matera β 355(D6)Met→Lys]: A new unstable hemoglobin variant in an Italian family. Hemoglobin 1990; 14: 79–85
  • 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: 137–145
  • Dash S., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Chandigarh or â2&94(FGl)Asp→Gly observed in an Indian family. Hemoglobin 1989; 13: 749–752
  • Jones R. T., Saointz H. I., Head C, Shin D. T. B., Fairbanks V. F. Hb Johnstown [β 109(Gll)Val→Leu]: A new electrophoretically silent variant that causes erythrocytosis. Hemoglobin 1990; 14: 147–156
  • Wajcman H., Mrad A., Blouquit Y., Parmentier C, Riou J., Galacteros F. Hemoglobin VUlejuif [β 123(H1) Thr→JJe]: A new variant found in coincidence with polycythemia vera. Am. J. Hematol 1989; 32: 294–297
  • Harano T., Harano K., Ueda S., Imai K., Marubashi S. Hb Yamagata [β 132(H10)Lys→Asn]: A new abnormal hemoglobin in a Japanese family. Hemoglobin 1990; 14: 207–211
  • Ulukutlu L., Ozsahin H., Wuson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Huisman T. H.J. Hb Brockton [â2β2138(H16)Ala-+Pro] observed in a Turkish girl. Hemoglobin 1989; 13: 509–513
  • Martins M. C., Rosado L., Wilson J. B., Kutlar A., Hu H., Huisman T. H.J. Hb Himeji or âβ 82140(H18)Ala→Asp in a Portuguese family. Hemoglobin 1989; 13: 411–415
  • Plaseska D., Li H-J., Wilson J. B., Kutlar F., Kutlar A., Huisman T. H. J., Kulpa J. Hb F-Brooklyn or â2gβ γ266 (E10)Lys→Gln. Hemoglobin 1990; 14: 213–216
  • 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: 734–736
  • Glader B. E. Hemoglobin FM-Fort Ripley: Another lesson from the neonate. Pediatrics 1989; 83: 792–793
  • Plaseska D., Kutlar F., Wilson J. B., Webber B. B., Zeng Y-T., Huisman T. H.J. Hb F-Jiangsu, the first 7 chain variant with a valine→methionine substitution: â2Aγ2134 (H12)Val→Met. Hemoglobin 1990; 14: 177–183
  • Harano T., Harano K., Doi K., Ueda S., Imai K., Ohba Y., Kutlar F., Huisman T. H.J. Hb F-Onoda or â2gγ2146 (HC3)His→Tyr, a newly discovered fetal hemoglobin variant in a Japanese newborn. Hemoglobin 1990; 14: 217–222
  • Codrington J. F., Kutlar F., Harris H. F., Wilson J. B., Stoming T. A., Huisman T. H.J. Hb Â2-Wrens or â2&298 (FG5)Val→Met, an unstable 5 chain variant identified by sequence analysis of amplified DNA. Biochim. Biophys. Acta 1989; 09(10)87–89
  • Wilson J. B., Webber B. B., Hu H., Kutlar A., Kutlar F., Codrington J.F, Prchal J. T., Hall K. M., de Pablos J.Ma., Rodriguez I., Huisman T. H.J. Hb Birmingham and Hb Galicia: two unstable β chain variants characterized by small deletions and insertions. Blood 1990; 75: 1883–1887
  • Ohba Y., Ami M., Imai K., Komatsu K., Amatsu K. Hb Masuda [β 114(G16)Leu→Met, 119(GH2)Gly→Asp], a hemoglobin with two substitutions in the 0 chain. Hemoglobin 1989; 13: 753–759
  • Wuson J. B., Webber B. B., Plaseska D., De Alarcon P. A., Mc Mulan S. K., Huisman T. H.J. Hb Davenport or â278(EF7)Asn→Hisβ2. Hemoglobin 1990; 14: 599–606
  • Ohba Y., Fujisawa K., Imai K., Leowattana W., Tani Y., Ami M., Miyaji T. A new or chain variant Hb Tonosho [allO(G17)Ala→Thr]: Subunit dissociation during cation exchange chromatography for Hb Afc assay. Hemoglobin 1990; 14: 413–422
  • Hidaka K., Iuchi I., Kobayashi T., Katoh K., Yaguchi K. Hb Fukutomi [â126(H9)Asp→Val]: A new hemoglobin variant with high oxygen affinity. Hemoglobin 1990; 14: 499–509
  • Plaseska D., Gu L-H., Wilson J. B., Codrington J. F., Huisman T. H. J., Dash S. Hb Sun Prairie or â2130(H13)Ala→Proβ2; second observation in an Indian adult. Hemoglobin 1990; 14: 491–497
  • 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 (â131[H14] Ser→Pro) and Hb Caen (âl32[H15]Val-Gly). Am. J. Hematol 1993; 42: 367–374
  • 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 [al35(H18)Val→Glu]. Clin. Chim. Acta 1990; 188: 39–48
  • Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K. A new hemoglobin variant, Hb Hanamaki or â2139(HCl)Gly→Glu β2, found in a Japanese family. Hemoglobin 1992; 16: 67–71
  • Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C, Blouquit Y., Craescu C. T., Galacteros F. Hb N-Timone [âβ28(A5) Lys→Glu]: A new fast-moving variant with normal stability and oxygen affinity. Hemoglobin 1989; 13: 743–747
  • 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 [â2BT254(D5)Val→Asp]: A new unstable variant found in a patient with hemolytic anemia. Hemoglobin 1990; 14: 653–659
  • Podda A., Galanello R., Maccioni L., Melis M. A., Rosatelli C, Perseu L., Cao A. Hemoglobin Cagliari β6O[E4]Val→Glu): A novel unstable thalassemic hemoglobinopathy. Blood 1991; 77: 371–375
  • Wajcman H., Kister J., Marden M., Bohn B., Blouquit Y., Descamps J., Goudemand M., Poyart C, Galacteros F. Hemoglobin Calais [j876(E20)Ala→Pro]: A hemoglobin variant with decreased intrinsic oxygen affinity. Biochim. Biophys. Acta 1991; 96(10)60–66
  • 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: 1150–1154
  • 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 [âβ87 (F3)Thr→Pro] and Hb F-Malta-I [â2gγ2117(G19)His→Arg] in the Maltese population. Hum. Genet. 1991; 86: 591–594
  • Wajcman H., Vasseur C, Blouquit Y., Esperito Santo D., Peres M. J., Martins M. C., Poyart C, Galacteros F. Hemoglobin Redondo [β 92(F8)His→Asn]: An unstable hemoglobin variant associated with heme loss which occurs in two forms. Am. J. Hematol. 1991; 38: 194–200
  • Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M. Hb Isehara (or Hb Redondo) [β 92(F8)His→Asn]: An unstable variant with a proximal histidine substitution at the heme contact. Hemoglobin 1991; 15: 279–290
  • Honig G. R., Vida L. N., Latorraca R., Divgi A. B. Hb South Milwaukee [β 105(G7)Leu→Phe]: A newly-identified hemoglobin variant with high oxygen affinity. Am. J. Hematol 1990; 34: 199–203
  • Harano T., Harano K., Kushida Y., Ueda S. A new abnormal variant, Hb Yahata or β 112(G14)Cys→Tyr, found in a Japanese: Structural confirmation by DNA sequencing of the j8-globin gene. Hemoglobin 1991; 15: 109–113
  • Plaseska D., Wilson J. B., Gu L-H., Kutlar F., Huisman T. H. J., Zeng Y-T., Shen M. Hb Zengcheng or âβ 2114(G16)Leu→Met. Hemoglobin 1990; 14: 555–557
  • Plaseska D., De Alarcon P. A., McMillan S., Walbrecht M., Wilson J. B., Huisman T. H.J. HbIowaorâβ 2119(GH2)Gly→Ala. Hemoglobin 1990; 14: 423–429
  • Abourzik N. N., Cordon M., Zordon G., Hine T. K., Johnson M. H., Jue D. L., Moo-Penn W. F. Hb St. Francis [β 121(GH4)Glu→Gly]: A new mutation at the same site as Hb D-Los Angeles. Hemoglobin 1991; 15: 115–117
  • Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., Lacombe C, Winichagoon P., Blouquit Y., Riou J., Wasi P., Galacteros F. Hemoglobin Dhonburi â2β2126(H4)Val→Gly: A new unstable 0 variant producing β -thalassemia intermedia phenotype in association with β °-thalassemia. Am. J. Hematol. 1990; 35: 96–99
  • Harano T., Harano K., Kushida Y., Ueda S. Structural analysis of abnormal hemoglobin by the polymerase chain reaction. Jap. J. Clin. Pathol. 1990; 38: 1067–1072
  • Plaseska D., Wilson J. B., Kutlar F., Font LI., Baiget M., Huisman T. H.J. Hb F-Catalonia or â2gγ215(A12)Trp→Arg. Hemoglobin 1990; 14: 511–516
  • 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: 509–515
  • 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: 393–405
  • 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 775 and a glycine residue in position γ136. Hemoglobin 1990; 14: 617–625
  • Harano T., Harano K., Kushida Y., Ueda S., Kawakami H. Hb A2-Niigata [→1(NAl)Val→Ala]: A new → chain variant found in the Japanese population. Hemoglobin 1991; 15: 335–339
  • Leung H., Gilbert A. T., Fleming P. J., Wong J., Hughes W. G., Hussein S., Nash A. R. Hb Â2-Parkville or →47(CD6)Asp→Val: A new 5 chain variant. Hemoglobin 1991; 15: 407–416
  • Plaseska D., Dimovski A. J., Wilson J. B., Webber B. B., Hume H. A., Huisman T. H.J. Hb 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: 178–181
  • 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: 529–5488
  • 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 â20293(F9)Cys-Arg; 121(GH4)Glu-Gln. Hemoglobin 1991; 15: 269–278
  • Coleman M. B., Steinberg M. H., Adams J. G., III. Hemoglobin Terre Haute [β 106 (G8) Arginine]: A posthumous correction to the original structure of Hb Indianapolis. Blood 1990; 76: 57a, Suppl. 1
  • Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., Harano K., Imai K. Hb Kanagawa [â40(C5)Lys→Met]: A new a chain variant with an increased oxygen affinity. Hemoglobin 1992; 16: 1–10
  • Zwerdling T., Williams S., Nasr S. A., Rucknagel D. L. Hb Port Huron [â56(E5)Lys→Arg]: A new â chain variant. Hemoglobin 1991; 15: 381–391
  • Perry M. C., Head C, Fairbanks V. F., Jones R. T., Taylor H., Proud V. Hemoglobin Columbia Missouri or â2[88(F9)Ala→Valβ2: A new high-oxygen-affinity hemoglobin that causes erythrocytosis. Mayo Clin. Proc. 1991; 66: 5–10
  • Langdown J. V., Davidson R. J. L, Williamson D. A new â chain variant, Hb Turriff [â99(G6)Lys→Glu]: the interference of abnormal hemoglobins in Hb Alc determination. Hemoglobin 1992; 16: 11–17
  • Fujisawa K., Hattori Y., Ohba Y., Ando S. Hb Yuda or â130(H13) Ala→Asp: A new â chain variant with low oxygen affinity. Hemoglobin 1992; 16: 435–439
  • Thein S. L., Best S., Sharpe J., Paul B., Clark D. J., Brown M. J. Hemoglobin Chesterfield (β 28 Leu→Arg) produces the phenotype of inclusion body β thalassemia. Blood 1991; 77: 2791–2793
  • 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 âβ232(B14)Leu→Val observed in an Arabian family in association with Hb S. Hemoglobin 1992; 16: 259–266
  • Molchanova T. P., Wilson J. B., Gu L-H., Guemira F., Fattoum S., Huisman T. H.J. Hb Bab-Saadoun or âβ248(CD7)Leu→Pro, a mildly unstable variant found in an Arabian boy from Tunisia. Hemoglobin 1992; 16: 267–273
  • 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 [β 81(EF5)Leu→His]. Biochim. Biophys. Acta, in press
  • 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 â2β299(Gl)Asp→Glu, a newly discovered high oxygen affinity variant. Hemoglobin 1991; 15: 487–496
  • Wajcman H., Kister J., Vasseur C, Blouquit Y., Behnken J. L., Galacteros F. Hb Ingelheim [β99(Gl)Asp→Glu]: A new high affinity hemoglobin variant destabilizing the al\32 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 [β 111(G13)Val→Ala]. Hemoglobin 1991; 15: 53–65
  • Pagano L., Lacerra G., Camardella L., De Angioletti M., Fioretti G., Maglione G., de Bonis C, Guarino E., Viola A., Cutolo R., DeRosa L., Carestia C. Hemoglobin Neapolis, \S126(H4)Val-β 31y: A novel β-chain variant associated with a mild β -thalassemia phenotype and displaying anomalous stability features. Blood 1991; 78: 3070–3075
  • Duwig I., North M. L., Barth J. G., Rieffel M., Nierengarten P., Arous N., Riou I., Galacteros F. Aspects hematologiques et anomalies structurales d'une nouvelle hemoglobine instable: L'Hb Sarrebourg β 8131(H9)Gln→Arg. Abstract. Nouv. Rev. Fr. Hematol 1987; 29: 344
  • Rahbar S., Lee T., Asmeron Y. Hb Beckman â2β2135(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 [β 3139(H17) Asn→Asp]. Hemoglobin 1991; 15: 85–95
  • 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 [β 143(H21)His→Asp]; a variant in the 2,3-DPG binding site showing normal oxygen affinity at physiological pH. Hemoglobin 1992; 16: 35–44
  • Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., Matsunaga T. Hb Kodaira [i3146(HC3)His→Gln]: A new β chain variant with an amino acid substitution at the C-terminus. Hemoglobin 1992; 16: 85–91
  • Park S. S., Barnetson R., Kim S. W., Weatherall D. J., Thein S. L. A spontaneous deletion of 033\34 Val in exon 2 of the β globin gene (Hb Korea) produces the phenotype of dominant j3 thalassaemia. Br. J. Haematol. 1991; 78: 581–582
  • 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 Zaire contains a five residue repetition within the a-chain and Hb Duino has two residues substituted in the β -chain. Hum. Genet. 1992; 78: 676–680
  • Trifillis P., Ioannou P., Schwartz E., Surrey S. Identification of four novel 5-globin gene mutations in Greek Cypriots using polymerase chain reaction and automated fluorescence-based DNA sequence analysis. Blood 1991; 78: 3298–3305
  • Abbes S., M'Rad A., Fitzgerald P. A., Dormer P., Blouquit Y., Kister J., Galacteros F., Wajcman H. Hb Al-Ain Abu Dhabi [â18(A16)Gly→Asp]: Anew hemoglobin variant discovered in an Emiratee family. Hemoglobin 1992; 16: 355–362
  • Curuk M. A., Altay C, Fei Y-J., Kutlar F., Baysal E., Gu L-H., Huisman T. H.J. Severe Hb H disease due to a combination of the -(â)20 kb deletion and Hb Adana, an unstable al variant with Gly→Asp at 59 (G→C GAC). Abstract. Blood 1992; 80: 81a
  • Ferranti P., Palapiano A., Malorni A., Pucci P., Marino G., Cossu G., Manca L., Masala B. Hemoglobin Ozieri: A new a-chain variant [â71(E20)Ala→Val]. Characterization using FAB-and electrospray-mass spectrometric techniques. Biochim. Biophys. Acta 1993; 116: 203–208
  • Wajcman H., Kister J., Galacteros F., Josifovska O., Spielvolgel A., Nagel R. L. Hb Montefiore [â126(H9)Asp→Tyr]: An abnormal hemoglobin with high oxygen affinity and absence of cooperativity. Abstract. Blood 1992; 80: 82a
  • Webber B. B., Wilson J. B., Gu L-H., Huisman T. H.J., Hb Ethiopia or
  • Wajcman H., Kister J., Marden M., Lahary A., Monconduit M., Galacteros F. Hemoglobin Rouen (â-140 (HC2) Tyr→His): alteration of the â-chain C-terminal region and moderate increase in oxygen affinity. Biochim. Biophys. Acta 1992; 80(11)53–57
  • 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 â2β 22(NÂ2)His→Leu; a new β chain variant observed in four families from Southern Austria. Hemoglobin 1992; 16: 493–501
  • 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 cisand a T→G mutation at codon 126 (Val→Gly; Hb Dhonburi) in transresulting in a thalassemia intermedia. Biochim. Biophys. Acta 1992; 80(11)173–179
  • Landin B. Hb Karlskoga or âβ e21(B3)Asp-His' a new slow-moving variant found in Sweden. Hemoglobin 1993; 17: 201–208
  • Ward CM., 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. NZJ. Med. 1992; 22: 390–391
  • 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 â2β 279(EF3)Asp→His (G. AOC Â): A stable hemoglobin variant with increased oxygen affinity observed in an Ethiopian male. Hemoglobin 1993; 17: 247–250
  • Broxson E. H., Hine T. K., Moo-Penn W. F. Hb Muskegon [β 83(EF7)Gly→Arg]: A new variant found in a family from the U.S. Hemoglobin 1993; 17: 85–86
  • de Castro CM., Lee M., Fleenor D. E., Devlin B., Kaufman R. E. A novel \3-globin mutation, β Durham-N.C. β 114)Leu→Pro], detected by SSCP, produces a dominant thalassemia-like phenotype. Abstract. Blood 1992; 80: 6a
  • Welch S., Bateman C. Hb D-Neath or β 121(GH4)Glu→Ala: A new member of the Hb D family. Hemoglobin 1993; 17: 255–259
  • Molchanova T. P., Postnikov Yu.V., Gu L-H., Huisman T. H.J. Hb Â2-Grovetown or â→275(E19)Leu-Val. Hemoglobin 1993; 17: 289–291
  • Saheki S., Ogawa Y., Nakaya K., Kohno T., Kuno T., Takaku T., Takahashi I., Shishino K., Takeuchi N. Hb Ehime or j357(El)-j358(E2) Asn-Pro→0, a new Bchain variant. Hemoglobin, in press
  • Merritt D., Jones R. T., Head C, Shih D., Xiao H., Thibodeau S. N., Fairbanks V. F. Hb Seal Rock: An extended achain variant associated with anemia microcytosis and a-thalassemia-2 (-3.7 kb). Hemoglobin, in press
  • Brennan S. O., Shaw J., Allen J., George P. M. β 141 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: 99–103
  • Brennan S. O., Shaw J. G., George P. M., Huisman T. H.J. Posttranslational modification of β 141 Leu associated with the β 75(E19)Leu→Pro mutation in Hb Atlanta. Hemoglobin 1993; 17: 1–7
  • 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 â7 globin gene produces a structural haemoglobin variant and a thalassemia. Br. J. Haematol. 1993; 84: 63, Suppl. 1
  • Bardakdjian J., Kister J., Wajcman H., Boulard P., Bohn B., Blouquit Y., Galacteros F. Hb Poitiers [a45(CE3)His→Asp]: A new hemoglobin variant with a two-fold increase in oxygen affinity. Hemoglobin, in press
  • Giordano P. C., Harteveld C. L., Streng H., Oosterwijk J. C., Heister J. G. A. M., Amons R., Bernini L. F. Hb Kurdistan [a47(CE5)Asp→Tyr], a new achain variant in combination with “-thalassemia”. Hemoglobin, in press
  • 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, a89 His→Leu) and athalassaemia 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 [â92(FG4) Arg→Trp]: A hemoglobin variant with a moderately increased oxygen affinity. Journees Scientifiques du Club de L'Hemoglobin. StrasbourgFrance June, 1993, Abstract.
  • Dinçol G., Dincol K., Erdem →., Pobedimskaya D. D., Molchanova T. P., Ye Z., Webber B. B., Wilson J. B., Huisman T. H.J. Hb Çapa or â294(Gl) Asp-Kilyfβ2, a mildly unstable variant with an A→G (G→C→G→C) mutation in codon 94 of the al-globin gene. Hemoglobin, in press
  • Morle F., Francina A., Philippe N., Souillet G., Godet J. Hb Sallanches, a new achain variant [â2 104(Gll)Cys→Tyr] associated with Hb H disease in one homozygous patient. Journees Scientifiques du Club de L'Hemoglobine. StrasbourgFrance June, 1993, Abstract
  • Wajcman H., Kalmes G., Groff P., Prome D., Riou J., Galacteros F. Hb Melusine [all4(GH2)Pro→Ser]: A new neutral hemoglobin variant. Hemoglobin 1993; 17: 397–405
  • Wajcman H., Kister J., M'Rad A., Marden M. C., Riou J., Galacteros F. Hb Val de Marne [â133(H16)Ser→Arg]: A new hemoglobin variant with moderate increase in oxygen affinity. Hemoglobin 1993; 17: 407–417
  • Owen M. C., Hendy J. G. Hb Footscray or â133(H16)Ser→Arg: A new hemoglobin variant. Hemoglobin, in press
  • Langdown J. V., Williamson D., Beresford C. H., Gibb I., Taylor R., Deacon-Smith R. A new β chain variant, Hb Tyne [β 5(Â2)Pro→Ser]. Hemoglobin, in press
  • Krishnan K., Martinez F., Cooney K., Jones R. T., Shih D. T., Dabich L. Co-inheritance of a low oxygen affinity hemoglobin, Hb Washtenaw, beta 11 (A8) Val-Phe and primary pulmonary hypertension in a Hungarian-American kindred. Blood 1993; 82: 471a, Suppl. 1
  • 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 âβ218(A15) Val→Gly, a silent, mildly unstable J3 chain variant detected by isoelectrofocusing and high performance liquid chromatography. Hemoglobin, in press
  • Coleman M. B., Adams J. G., Smith CM., Steinberg M. H. Modulation of Hb Koln disease by an additional mutation: Hb Medicine Lake. Blood 1993; 82: 222a, Suppl. 1
  • Owen M. C., Ockelford P. A., Wells R. M.G. Hb Howick [β 37(C3)Trp→Gly]: A new high oxygen affinity variant of the âβ 1 contact. Hemoglobin, in press
  • Stabler S., Jones R. T., Head C, Shih D. T. B., Fairbanks V. F. Hemoglobin Denver, beta 41(C7) Phe→Ser: A low β2 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 â2β267(El l)Val→Met: A new unstable hemoglobin variant identified through sequencing of amplified DNA. Hemoglobin 1993; 17: 217–225
  • 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 β 67(Ell)Val-Gly: Transfusion-dependent haemolytic anaemia ameliorated by coexisting alpha thalassemia. Br. J. Haematol. 1993; 85: 352–355
  • Wajcman H., Kister J., Prome D., Galacteros F., Gilsanz F. Hb Villaverde β 389(F5)Ser→Arg]: the structural modification of an intrasubunit contact is responsible for a high oxygen affinity. Biochim. Biophys. Acta, in press
  • Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T. P., Huisman T. H.J. Hb Hradec Kralove (Hb HK) or Lβ2115(G17)Ala→Asp, a severely unstable hemoglobin variant resulting in a dominant β -thalassemia trait in a Czech family. Hemoglobin 1993; 17: 319–328
  • Girodon E., Ghanem N., Vidaud M., Riou J., Martin J., Galacteros F., Goossens M. Rapid molecular characterization of mutations leading to unstable hemoglobin \3-chain variants. Ann. Hematol. 1992; 65: 188–192
  • North M. L., Duwig I., Kister J., Bergerat J. P., Oberling F., Groell J. J., Lampert E., Lonsdorfer J., Galacteros F. Hb Puttelange [β 14O(H18) Ala→Val]: Anew high oxygen affinity variant identified by mass\mass spectrometry. Journees Scientifiques du Club de L'Hemoglobin. StrasbourgFrance June, 1993, Abstract
  • Pobedimskaya D. D., Molchanova T. P., Huisman T. H. J., Harding S. R., Bakanec R. Hb F-Saskatoon or â2gγ221(B3)Glu→Lys observed in a North American Indian newborn. Hemoglobin, in press
  • Pobedimskaya D. D., Molchanova T. P., Gu L-H., Molina M. A., de Pablos J.Ma, Huisman T. H.J. Hb F-Sacromonte or â27259(E3)Lys→Gln observed in a Spanish newborn and his mother. Hemoglobin 1993; 17: 269–274
  • Ferranti P., Barone F., Pucci P., Malorni A., Marino G., Manca L., Masala B. Hb F-Sassari: A novel gγ variant with a threonine residue in position γ75 characterized by mass spectrometric techniques. Hemoglobin, in press
  • 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 Â2-Liangcheng [→117(G19)Asn→Asp (→→Â)]: A new → chain variant detected by gene analysis in a Chinese family. Hemoglobin 1993; 17: 463–466
  • Girodon E., M'Rad A., Martin J., Goossens M., Galacteros F., Rosa J., Gisselbrecht C, Boiron M., Cohen I. J., Jaber L., Tamari H., Goshen J., Zaizov R., Wajcman H. Hb Taybe (â38 or 39 Thr deleted): A new unstable alpha chain hemoglobin variant. Blood 1992; 80: 388a, Suppl. 1
  • Fujisawa K., Yamashiro Y., Hattori Y., Ohba Y., Kajita T., Kageyama S., Arita J. Hb Higashitochigi (Hb HT) [β24(B6) or β 25(B7) glycine deleted]: A new unstable variant expressing cyanosis. Hemoglobin 1993; 17: 467–473

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:

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:

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.