International Hemoglobin Information Center

References

• Crookston J. H., Beale D., Irvine D, Lehmann H. A new Haemoglobin, J Toronto (α5 Alanine → Aspartic acid). Nature, London 1965; 208: 1059–1061
   PubMed Web of Science ®Google Scholar
• Sumida I., Ohta Y., Imamura T., Yanase T. Hemoglobin Sawara: α6 (A4) Aspartlc acid → Alanine. Blochim. Biophys. Acta 1973; 322: 23–26
   PubMed Web of Science ®Google Scholar
• Pootrakul S., Kematorn B., Na-Nakorn S., Suanpan S. A new haemoglobin variant: Haemoglobin Anantharaj alpna 11 (A9) Lyaine→Glutalanic acid. Biochim. Biophys. Acta 1975; 405: 161–166
   PubMed Web of Science ®Google Scholar
• Rosa J., Maleknia N., Vergoz D., Dunet R. Une nouvelle hémoglobine anormale: 1'hémoglobin Jα Paris 12 Ala→Asp. Nov. Rev. Fr. D'Hemat. 1965; 6: 423–426
   Google Scholar
• Trincao C., Martins De Melo J., Lorkin P. A., Lehmann H. Haemuglobin J Paris in the south of Portugal (Algarve). Acta Hnemat 1968; 39: 291–298
   PubMed Web of Science ®Google Scholar
• Marti H. R., Pik C., Mosimann P. Eine Neue Hämoglobin I - variante: lib I Interlaken. Acta Haemat 1964; 32: 9–16
   PubMed Web of Science ®Google Scholar
• Liddell J., Brown D., Beale D., Lehmann H., Huntsman R. G. A new haemoglobin - Jα Oxford found during a survey of an Englisn population. Nature, London 1964; 204: 269–270
   PubMed Web of Science ®Google Scholar
• Silvestroni E., Bianco L., Tentori L., Vivaldi C., Carta S., Sorcini M., Brancati C (1967) Proc. 10th Congr. Europ. Soc. Haemat., Strasbourg, 1963. Karger, Basel/New York, pp. 232–237, part 11
   Google Scholar
• Vella F., Casey W., Lehmann R., Labossiere A., Jones T. C. Haemoglobin Ottawa: α2 15(A13) Cly→Arg 82. Biochim. Biopliys. Acta 1974; 336: 25–29
   Web of Science ®Google Scholar
• Pootrakul S., Srichiyanont S., Wasi P., Suanpan S. Hemoglobin Siam (α2 15 Arg β2): A new a chain variant. Humangenetik 1974; 23: 199–204
   PubMedGoogle Scholar
• Beale D., Lehmann E. Abnormal haemogloblns and the genetic code. Nature 1965; 207: 259–261
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Alperin J. B., Beale D., Lehmann H. Hemoglobin I in an American Black family: Structural and hematulogic studies. J. Lab. Clin. Med. 1966; 68: 940–946
   PubMed Web of Science ®Google Scholar
• Bovman B. H., Rarnett D. R. Amino-acid substitution in Haemoglobin I (Texas variant). Nature 1967; 214: 499
   Web of Science ®Google Scholar
• O'Brien C., Gray M. J., Jacobs A. S. A survey of cord bloods for abnormal hemoglobin with further observations on hemoglobin I. Am., J. Obst.& Gynec. 1964; 88: 816–822
   PubMed Web of Science ®Google Scholar
• Raur E. W. Hb α2gluβ2 (lib I) in a Caacasian Eamily: independent mutation or common origin. Humangenetik 1968; 6: 368–372
   PubMedGoogle Scholar
• Griffiths K. D., Lang A., Lehmann H., Mann I. R., Plowman D., Raine D. N. Haemglobin Handsuorth α18 (A16) Glycine → Arginine. FEBS Letters 1977; 75: 93–95
   PubMed Web of Science ®Google Scholar
• Rahbar S., Ale F., McHavan E., Nowzari G., Shoa'i I., Zamanianpoor W. H. Two new haemoglohins: Haemglobin Perspolis (α64 (E13) Asp→Tyr] and Haemoglobin J-Knrosh [α19 (AB) Ala→Asp]. Biochim. Biophys. Acta 1976; 9: 119–125
   Google Scholar
• Kendall A. C., Barr R. D., Lane A., Lehmann H. Haemglobin J Nyanza: α21 (B2) Ala→Asp. Biochim. Biophys. Acta 1973; 310: 357–359
   PubMed Web of Science ®Google Scholar
• Gottlieb A. J., Restrepo A., Itano H. A. Hemoglohin J Medellin. Chemical and genetic study. Fed. Proc. 1964; 23: 172
   Google Scholar
• Kraus A. P., Mlyaji T., Iuchi I., Kraus L. M. Memphis. A new variety of sickle cell anemia with clinically mild symptoms due to an α-chain variant of hemoglobin (α23Glu N112). J. Lab. Clin. Pled. 1965; 66: 866–887
   Web of Science ®Google Scholar
• Boyer S. H., Crosby E. F., Fuller C. F., Ulenurm L., Buck A. A. A survey of hemoglobins in the Republic of Chad and characterization of hemoglobin Chad: α2 23Glu→Lys β2. Amer. J. Human Genet. 1968; 20: 570–578
   PubMed Web of Science ®Google Scholar
• Marengo-Rowe A. J., Beale D., Lehmann H. New human haemnglohin variant from Southern Arahia: G-Audhali (α23 (B4) Glutanic acid→Valine) and the variabllity of B4 in human haemglobin. Nature, tondon 1968; 219: 1164–1166
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Brimhall B., Jones R. T., Bryant R., Mitchell C. B., Goldberg A. I. Hb Fort Worth: α27 Glu→Gly (B8) a variant present in unusually low concentration. Biochirn. Biophys. Acta 1971; 243: 164–169
   PubMed Web of Science ®Google Scholar
• Ahern E., Ahern V., Hulder W., Palomino E., Serjeant G. R., Serjeant B. E., Forbcs M., Brimhall B., Jones R. T. Haewglobin Spanish Town α27 Glu→Val (88). Biochim. Biophys. Acta 1976; 427: 510–536
   Google Scholar
• Vettore L., DeSandre G., Dilorio E. E., Wlnterhalter K. H., Lang A., Lehmann H. A new abnormal Hemoglobin O Padova, α30 (B11) Glu→Lys and a dyserythropoietic anemia with erythroblastic multiuuclearity co-existing in the same patlent. Blood 1974; 44: 664–377
   Web of Science ®Google Scholar
• Schneider R. C., Jim R. T.S. A new haemoglobin variant (the ‘Ronolulu Type’) in a Chinese. Nature 1961; 190: 454–455
   PubMed Web of Science ®Google Scholar
• Vella Y., Ager J. A.M., Lehmann H. An abnormal haemoglobin in a Chinese: Haemoglobin G. Nature 1958; 182: 460–461
   PubMed Web of Science ®Google Scholar
• Swenson R. T., Bill R. L., Leamann →., Jim R. T.S. A chemical abnormality in Hemoglobin G from Chinese Individuals. J. Blol. Chem. 1962; 237: 1517–1520
   Web of Science ®Google Scholar
• Beretta A., Prato V., Gallo E., Lehmann It. Haemoglobin Torino - α43 (CDI) Phenylalanine→Valine. Nature, London 1968; 217: 1016–1018
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Yokoyama K., Numakura H., Nagata K., Takebe Y., Izumi Y., Shibata S. Hemoglobin Hirosaki (α43[CE 1]Phe→Leu), a new unstable variant. Bloclilm. Biophys. Acta 1975; 405: 155–160
   PubMed Web of Science ®Google Scholar
• Sumida I. Studies of abnormal hemoglobins in western Japan
   Google Scholar
• Fujlmura T., Kawasaki C., Imamura T., Ohta Y., Hanada M., Yanmoka K. Two kindreds of abnormal hemoglobin: Hb Tagawa I amd Hb Tagawa II. Jap. J. Clin. Hemat. 1964; 6: 71
   Google Scholar
• DeVries A., Joshua H., Lehmann H., Hill R. L., Fellows R. E. The first observation of an abnormal haemoglobin in a Jewfsh family: Haemylobin Beilioson. Brit. J. Haemat. 1963; 2: 434–486
   Google Scholar
• Halbrecht L., Isaacs W. A., Lehmann H., Ben-Porat F. Hemoglobin Rasharon (α47 Aspartic acid→Histidime) Israel J. Med. Sci. 1967; 3: 827–831
   Google Scholar
• Ostertag W., Smith E. W. Hb Sinai, a new a chain mutant α47 His. Humangenetik 1962; 5: 377–379
   Google Scholar
• Schneider R. G., Ueda S., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sealy (α247Hisβ2) : a new variant in a Jewish family. Am. J, Human Genet. 1968; 20: 151–156
   PubMed Web of Science ®Google Scholar
• Eianco J., Modiano G., Botthi E., Lucci R. Alteration in the α-clinin of Haemoglobin L Ferrara. Nature, London 1963; 198: 395–396
   PubMedGoogle Scholar
• Tentori L. Henoglobin L Ferrara = Hemoglobin Hasliaron. Hemglobin (This issue) 1977
   Google Scholar
• Rahbar S., Mahdavi N., Nowzari G., Hostnfavi I. Hemoglobin Arya: α247(CD5) Aspartic acid→Asparagine. Riochim. Biophys. Acta 1975; 386: 525–529
   PubMed Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Schneider R. G., Hosty T. S., Tomlin G., Atkins R. Two new hemoglobins: Hemoglobin Alabama (839(C5)Gln→Lye) and Henmglobin Montgomery (α48(CD6)Leu→Arg). Biochim. Biophys. Acta 1975; 379: 28–32
   PubMed Web of Science ®Google Scholar
• Tangheroni W., Zorcolo G., Gallo E., Lehmann H. Haemoglobin J Sardegnn: α50 (CD8) Histidine → Aspartic acid. Nature, London 1968; 218: 470–471
   PubMed Web of Science ®Google Scholar
• Cnbannes R., Renaud R., Flauran A., Pennors H., Charleswrth D., Price B. C., Lehmann H. Deux ténoglobines rapides an Cbte-D'Ivoire: 1'Hb K Woolwfch et une nouvelle hémoglobine, l'Hb J Abidjan (α51 Gly→Asp). Nouv. Revue Pr. Hemat. 1972; 12: 289–300
   PubMedGoogle Scholar
• Reynolds C. A., Huisman T. R.J. Hemoglobin Russ or α2 51Arg β2. Biochim. Biophys. Acta 1966; 130: 541–543
   PubMed Web of Science ®Google Scholar
• Alberti R., Mariuzzi C. H., Artibani L., Bruni I., Tentori L. A new baemoglobin variant: J-Rovigo alpha 53 (E-2) alanine → aspartic acid. Blochim. Biophys. Acta 1974; 342: 1–4
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Takeda I., Shibnta S. Hemoglobin Shimonoseki (α2 54Arg β2A), a slow-moving hemoglobin found in a Japanese family, with special reference to its chemistry. Acta Haen. Jap. 1963; 26: 531–537
   PubMedGoogle Scholar
• Jones R. T., Brimhall R., Lisker R. Chemical characterieation of Hemoglobin Mexico and Hemoglobin Chiapas. Biochim. Biophys. Acta 1968; 154: 486–495
   Google Scholar
• Rosa J., Lable D., Maleknla N., Blum N. Sur quelques hémoglobines anormales nouvelles recemment isolées en France. International Symposium on Comparative Hemoglobin Structure. Thessalaniki. 11–13 April, 1966, p. 140–145
   Google Scholar
• Fessas Ph., Kaltsoya A., Loukopoulos D., Nilsson L. O. On the chemical structure of Haemoglobin Uppsala. Human Heredity 1969; 19: 152–151
   PubMed Web of Science ®Google Scholar
• Rahbar S., Kinderleret J. L., Lehmann H. Haewglobin L Persian Gulf: α57 (E6) Glyclne → Arginine. Acta Haemat 1969; 42: 169–175
   PubMed Web of Science ®Google Scholar
• Baglioni C. A chemlcal study of Hemoglobin Norfolk. J. Biol. Chem. 1962; 237: 69–74
   PubMed Web of Science ®Google Scholar
• Imamura T. Hemoglobin Kagoshima: An example of Hemoglobin Norfolk in a Japanese family. Amer. J. Human Genet. 1966; 18: 584
   PubMed Web of Science ®Google Scholar
• Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb If. Proc. Nat. Acad. Sci. (Wash.) 1961; 47: 1758–1767
   PubMed Web of Science ®Google Scholar
• Shimizu A., Hayashl A., Yamamura Y. The structural study on a new hemglobin variant, Hb M Osaka. Biochim. Biophys. Acta 1965; 97: 472–482
   PubMed Web of Science ®Google Scholar
• Hansen H. A., Jagenburg O. R., Johansson B. G. Studies on an abnormal hemoglobin causing hereditary congenital cyanosts. Acta Paediatrica 1960; 49: 503–511
   PubMedGoogle Scholar
• Hollán S. R., Szelényi J. C., Lehmann H., Beale D. A Boston-type haemoglobin M in Hungary: Haemoglobin M Kiskunhaias. Haematologia 1967; 1: 11–18
   Google Scholar
• Barclay G. P.T., Charlesworth D., Lehmann H. Abnormal haenoglobins In Zambia. A new Uaemoglobin Zambia α60 (E9) Lyslne → Asparaginc. Brit. Med. J. 1969; 4: 595–596
   PubMed Web of Science ®Google Scholar
• Brimhall B., Duerst M., Hollán S. R., Stenzel P., Szelényl J., Jones R. T. Structural characterizations of Hemoglobins J Buda (α6) (E10) Lys→Asn) and G Pest (α74 (EF3) Asp→Asn). Biochim. Biophye. Acta 1974; 336: 344–360
   Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T.S., Tan T. G.H., Weng M. I., Liu C. S., Wsng C. L. Heamoglobin G Waimanalo: α64 Asp→Asn. Biochim. Biophys. Acta 1973; 322: 27–33
   PubMed Web of Science ®Google Scholar
• Ramot B., Rlnderlerer J. B., Lehmann H. Geneva 1972, Cited in WHO Technlcal Report Series No. 509, Annex 1
   Google Scholar
• Sukumaran P. K., Merchant S. M., Desai M. P., Wiltshire B. G., Lehmann H. Haemglobin Q (α64 (E13) Aspartic acid → Histidine) associated with β-thalassemia in three Sindhi families. J. Med. Genet. 1972; 9: 436–442
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Yamamoto K., Ohba Y., Shibata S. Amino acid substitution of Hemoglobin Ube 2 (α2 68Asp β2): an example of successful application of partial hydrolysis of peptide with 5% acetic acid. Clin. Chim. Acta 1967; 16: 347–352
   PubMed Web of Science ®Google Scholar
• Baglioni C., Ingram V. H. Abnormal Human Haemoglobins V. Chemical investigation of Haemglobins A, G, C, X from one individual. Biochim. Biophys. Acta 1961; 48: 253–265
   PubMed Web of Science ®Google Scholar
• Chernoff A. I., Pettit N., Jr. The amino acid composition of hemoglobin VI. Separation of the tryptic peptides of Hemoglobin Knoxville No. I on Dowex-I X-2 and Sephadex. Biochim. Biophys. Acta 1965; 97: 47–60
   PubMed Web of Science ®Google Scholar
• Bowman B., Barnett D. R., Hodgkinson K. T., Schneider R. G. Chemical characterization of Haemglobin G St-I. Nature 1966; 211: 1305–1306
   PubMed Web of Science ®Google Scholar
• Minnich V., Cordonnier J. K., Williams W. J., Moore C. V. Alpha, beta and gamma hemoglobin polypeptide chains during the neonatal period with description of a fetal form of Hemoglobin D St. Louis. Blood 1962; 19: 137–167
   PubMed Web of Science ®Google Scholar
• Dance N., Huehns E. R., Shooter E. M. The chemical investigation of Hemglobins G Bristol and G Briatol C. Biochim. Biophys. Acta 1964; 86: 144–148
   PubMed Web of Science ®Google Scholar
• Colombo B., Vidal G., Kamuzora H., Lehmann H. A new haemglobin J-Habana α71 (E2O) Alanim → Glutamic acid. Biochim. Biophys. Acta 6, 351: 1–6
   Google Scholar
• Rahbar S., Nowtari C., Danèshmand P. Haemoglobin Daneshgah-Tehran α2 72(EFI) Histidine → Arginine β2A. Nature New Biology 1973; 245: 268–269
   PubMedGoogle Scholar
• Pootrakul S., Dixon G. H. Hemoglobin Mahidol: a new hemoglobin α-chain mutant. Canad. J. Biochem. 1970; 48: 1066–1078
   Web of Science ®Google Scholar
• Blackwell R. Q., Liu C. S. Hemoglobin G Taichung: α74 Asp→ His. Biochim. Biophys. Acta 1970; 200: 70–75
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Charlesworth D., Lehmann H., Rahbar S., Tuchinda S. Lie Injo, Luan Eng Two Haeonoglobins Q, α74(EF3) and α75(EF4) Aspartic acid → Histidine. Brit. J. Haemat. 125, 19: 117–125
   Google Scholar
• Orringer E. P., Wlilson J. B., Huismen T. H.J. Hemoglobin Chapel Hill or α2 74 Asp→Gly β2. FEBS Letters 1976; 65: 297–300
   PubMed Web of Science ®Google Scholar
• Vella F., Wiltshire B. G., Lehmann H., Galbraith P. Hemoglobin winnlpeg: α2 75 Asp→Tyr β2. Clin. Biochem. 1973; 6: 66–10
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyajt T., Matsuoka M., Takeda I., Fukuba Y., Shibata S., Obkura K. Heaoglobin Matsue-Oki: alpha 75 (EF 4) Aspartic acid → Asparagiue. Hemogiobin 1977; 1: 383–388
   PubMed Web of Science ®Google Scholar
• Van Ros G., Beale D., Lehmann H. Haemglobin Stanieyville 11 (α78 Asparagine → Lysine). Brit. Med. J. 1968; 4: 92–93
   PubMed Web of Science ®Google Scholar
• Rucknagel D. L., Brandt H. J., Spencer H. H. α-chain mutants of human hemoglobin contributing to the genetics of the α-chain locus. Proc. 1st Inter-American Symp. Hemoglobins, Caracus, 1969
   Google Scholar
• Adams J. C., III, Winter W. P., Ruchagel D. L., Spencer H. H. Biosyathesis of Hemoylobln Ann Arbor: Evidence for catabolic and feedback regulation. Science 1972; 176: 1427–1429
   PubMed Web of Science ®Google Scholar
• Winter W. P, Personal communication
   Google Scholar
• Crookston J., II., Parquliarson H. A., Beale D., Lehmann H. ttemoglobin Etobicoke: a84 (F5) Serine replaced by Arginine. Canad. J. Bfochen. 1969; 42: 143–146
   Google Scholar
• Lorkin P. A., Huntsman B. C., Ager J. A.M., Lelimann H., Vella F., Darbra P. 0. ttaemoglobin C Norfolk: a85 (F6) AspAsn. Biochim. Biophys. Acta 1975; 2: 22–27
   Google Scholar
• Cotten-Solal M., Hanesse B., Tttillet J., Rosa J. Haemoglobln C Norfolk u85 (F6) AspAsn. Structural cliaracterization by soquenator analysis and functional properties of a new variant with high oxygen affinity. FEBS Letters 1975; 2: 163–167
   Google Scholar
• Fujiwara H., Maekawa T., Matsuda G. Hemoglobin Atago (α2 85 Tyr β2) a new abnormal human hemoglobin found in Nagasaki. Int. J. Protein Research 1971; 3: 35–39
   PubMedGoogle Scholar
• Reed R. E., Winter W. P., Rucknagel D. L. Haemglobin Inkster (α2 85 Aspartic acid → Valine β2) coexisting with β-thalassemia in a Caucasian family. Brit. J. Haemat. 1974; 26: 475–464
   PubMed Web of Science ®Google Scholar
• Miyaji T., Iuchi I., Shibata S., Takeda I., Tamura A. Possible amino acid substitution in the α-chain (α67 Tyr) of Hb M Iwate. Acta Haem. Jap. 1963; 26: 538–543
   PubMedGoogle Scholar
• Heller P., Weinstein R. C., Yakulis V. J., Rosenthal I. M. Hemoglobin M Kankakee, a new variant of Hemoglobin M. Blood 1962; 20: 287–301
   PubMed Web of Science ®Google Scholar
• Pik C., Tönz O. Nature of Haemoglobin M Oldenburg. Nature 1966; 210: 1182
   PubMed Web of Science ®Google Scholar
• De Traverse P. M., Lehmann H., Coquelet M. L., Beale D., Isaacs W. A. Etude d'une hémoglobine Jα non encore décrite, dans une famille francais. Compt. R. Scéanc. Soc. Biol. 1966; 160: 2270–2272
   PubMed Web of Science ®Google Scholar
• Vella F., Charlesworth D., Lorkin P. A., Lehmann H. Hemoglobin Broussais: α→Lys→Asn. Can. J. Biochem. 1970; 43: 908–910
   Google Scholar
• Braconniet F., Cohen-Solal M., Schiegel N., Blauquit Y., Thillet J., Cassius De Linval J., Rosa J. Hemoglobine J Broussais α2 90 Lys→Aun β2A (FG2), decouverte dans une famille Martiniquaise. Nouvelle Revue Française d'Hematologie 1975; 3: 333–342
   Google Scholar
• Hyde R. D., Kinderlerer J. L., Lehmann H., Hall M. D. Haemoglobin J Rajappen: α90 (FG2) Lyn→Thr. Biochim. Biophys. Acta 1971; 243: 515–519
   PubMed Web of Science ®Google Scholar
• Botha M. C., Beale D., Isaacs W. A., Lehmann H. Haemoglobin J Cape Town α2 92 Arginine → Glutamine β2. Nature, London 1966; 212: 792–795
   PubMed Web of Science ®Google Scholar
• Lines J. G., McIntosh R. Oxygen binding by Haemoglobin J Cape Town (α2 92 Arg→Gln). Nature 1967; 215: 297–298
   Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal human haemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol. 1966; 19: 91–108
   PubMed Web of Science ®Google Scholar
• Charache S., Weatherall D. J., Clegg J. B. Polycythemia associated with a hemoplobinopathy. J. Clin. Invest. 1966; 45: 813–822
   PubMed Web of Science ®Google Scholar
• Wajcman U., Belkhodja O., Labie D. Hb Setif: Gl(94) αAsp→Tyr. A new α chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits. FEBS Letters 300, 27: 298–300
   Google Scholar
• Schaeider R. G., Atkins R. J., Hosty T. S., Tomlin G., Casey R., Lehmann I L., Lorkin P. A., Nagai K. Haemoglobin Titusville: α94 Asp→Asn, a new haemglobin with a lowered affinity for oxygen. Biochim. Biophys. Acta 1975; 400: 365–373
   PubMedGoogle Scholar
• Huisman T. H.J., Adams H. R., Wilson J. B., Efremov G. D., Reynolds C. A, Wrightstone R. N. Hemoglobin G Georgia or- α2 95Leu (G2)β2. Biochia. Blophys. Acta 1970; 200: 578–5180
   PubMed Web of Science ®Google Scholar
• Smith L. L., Plese C. L., Barton B. P., Charache S., Wilson J. B., Huisman T. H.J. Subunit dissociation of the abnormal hemoglobins G Georgia (α2 95 Leu (G2)β2) and Rampa (α2 95Ser (G2)β2). J. Biol. Chem. 1972; 247: 1433–1439
   PubMed Web of Science ®Google Scholar
• De Jong W. W.W., Bernini L. F., Khan P. H. Haemglobin Rampa: α95 Pro→rSer. Biochim. Biophys. Acta 1971; 236: 197–200
   PubMed Web of Science ®Google Scholar
• Wiltshire B. G., Clark K. G.A., Lorkin P. A., Lehmann H. Haemoglobin Denmark Hill α95 (G2) Pro→Ala, a variant with unusual electrophoretic and oxygen binding properties. Biochim. Biophys. Acta 1972; 278: 459–464
   PubMed Web of Science ®Google Scholar
• Bannister W. H., Crech J. L., Plese C. F., Smith L. L., Barton B. P., Wilson J. B., Reynolds C. A., Huisman T. H.J., Hemoglobin St. Luke's or α2 95 Arg (G2) β2. European J. Biochem. 1972; 29: 301–307
   PubMedGoogle Scholar
• Crookston J. H., Farquharson H., Kinderlerer J., Lehmann H. Hemoglobin Manitoba: α102 (G9) Serine replaced by Arginine. Canad. J. Boochem. 1970; 48: 911–914
   PubMedGoogle Scholar
• Charache S., Ostertag W. Hemoglobin Hopkins-2 ((α112 Asp)2 β2): “Lou Output” protects from potentially harmful effects. Blood 1970; 36: 852
   Google Scholar
• Niazi G. A., Efremov C. D., Nikolov N., Hunter E., Jr., Luisman T. II.J. Hemoglobin Strumica or α2 112(G19)Htis→Argβ2. (With an addendum: Hemoglobin- J Paris-I. α2 12(A10)Ala→Aspβ2 in the same population). Eiochim. Biophys. Acta 1975; 412: 181–186
   PubMed Web of Science ®Google Scholar
• Beksedic D., Rajevska T., Lorkin P. A., Lehmann H. Hb Serbia (α1 1 2(G19)llis→Arg), a new haemoglobin variant from Yugoslavia. FEBS Letters 1975; 58: 226–229
   PubMed Web of Science ®Google Scholar
• Gajdusek D. C., Guiart J., Kirk R. L., Carrell R. W., Irvine D., Kynoch P. A.M., Lehmann H. Haemoglobin J Tongariki (α115 Alanine → Aspartic acid): the first new haemoglobin variant found in a Pacific (Melanesian) population. J. bled. Genet. 1967; 4: 1–6
   Google Scholar
• Baglioni C., Lehmann I L. Chemical heterogeneity of Haemoglobin 0. Nature 1962; 196: 229–232
   PubMed Web of Science ®Google Scholar
• Lie-Injo Luan Eng, Sadono Haemoglobin 0 (Buginese X) in Sulawesi. Brit. Med. J. 1958; i: 1461–1462
   Google Scholar
• Sansone G., Centa A., Sciarratta V., Gallo E., Lehmann H. llaemoglobin O Indonesia (α116Glu→Lys) in an Italian family. Acta Haemat 1970; 43: 40–47
   PubMed Web of Science ®Google Scholar
• Ostertag W., von Ehrenstein G., Charache S. Duplicated α-chain genes in Hopkins-2 Haemoglobin of man and evidence for unequal crossing over between them. Nature New Biology 1972; 237: 90–94
   PubMedGoogle Scholar
• Blackwell R. Q., Wong H. B., Wang C. L., Weng M. L, Liu C. S. Hemoglobin J Meerut: α120 Ala→Glu. Biochim. Biophys. Acta 1974; 351: 7–12
   PubMed Web of Science ®Google Scholar
• Kamuzora H., Lehmann H., Griffiths K. D., Mann J. R., Roine D. N. A new haemglobin variant Haemoglobin J Birminghan α120 (113) Ala→Glu. Ann. Clin. Biochem. 1974; 11: 53–55
   Web of Science ®Google Scholar
• Moo-Penn W. F., Jue D L., Johnson M. H., Wilson S. M., Therrell B., Jr., Schmidt R. M. Hemoglobin Tarrant: α126(H9)Aap→Asn. A new hemoglobin variant in the α1β1 contact region showing high oxygen affinity and reduced cooperativity. Biochim. Biophys. Acta 1977; 490: 443–451
   PubMed Web of Science ®Google Scholar
• Vella F., Galbraith P., Wilson J. B., Wong S. C., Folger G. C., Huisman T. H.J., Hemoglobin St. Claude or α2 127 (H10)Lys→Thr β2. Biochim. Biophys. Acta 1974; 365: 318–322
   PubMed Web of Science ®Google Scholar
• Moo-Pen W. F., Bechtel R. C., Johnson M. H., Jue D. L., Holland S., Huff C., Schmidt R. M. Hemoglobin Jackson, α127(HlO)Lys→Asn. A. J. C. P. 1976; 66: 453–456
   Google Scholar
• Klethauer E. P., Reynolds C. A., Dozy A. M., Wilson J. B., Moores R. R., Bereason M. P., Wrights C. S., Huisman T. B.J. Hemoglobin Bibba or α2 136 Pro β2, an unstable α-chain abnorwal hemoglobin. Biochim. Biophys. Acta 1968; 154: 220–222
   PubMedGoogle Scholar
• Clegg J. B., Weatherall D. J., Boon Wong Hock, Mustafa D. Two new haemglobin variants involving proline substitutions. Nature, London 1969; 222: 379–380
   PubMed Web of Science ®Google Scholar
• Poyart C., Krishnamoorthy R., Bursaux E., Gacon G., Labie D. Structural and functional studies of Haemoglobin Suresnes or α2 141 (llC3) Arg→llisβ2, a new high oxygen affinity mutant. FEBS Letters 1976; 69: 103–107
   PubMed Web of Science ®Google Scholar