International Hemoglobin Information Center: Policies -Ihic

References

• Moo-Penn W. F., Bechtel K. C., Schmidt R. M., Johnson M. H., Jue D. L., Schmidt D. E., jr, Dunlap W. M., Opella S. J., Bonaventura J., Bonaventura C. Hemoglobin Raleigh (β1 Valine→Acetylalanine). Structural and Functional Characterization. Biochemistry 1977; 16: 4872–4879
   PubMed Web of Science ®Google Scholar
• Labossiere A., Vella F., Hiebert J., Galbraith P. Hemoglobin Deer Lodge: α2β2 His→Arg. Clin. Biochem. 1972; 5: 46–50
   PubMed Web of Science ®Google Scholar
• Ingram V. M. Abnormal Human Haemoglobins. III. the chemical difference between normal and sickle cell haemoglobins. Biochim. Biophys. Acta 1939; 36: 402–411
   Google Scholar
• Hunt J. A., Ingram V. M. Abnormal Human Haemoglobins. IV. the chemical difference between normal human haemoglobin and Haemoglobin C. Biochim. Biophys. Acta 1960; 42: 409–421
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Oemijati S., Pribadi W., Weng M.-I., Liu C.-S. Hemoglobin G Makassar: β6 Glu→Ala. Biochim. Biophys. Acta 1970; 214: 396–401
   PubMed Web of Science ®Google Scholar
• Hill R. L., Swenson R. T., Schwartz H. C. Characterization of a chemical abnormality in Hemoglobin G. J Biol. Chem. 1960; 235: 3182–3187
   PubMed Web of Science ®Google Scholar
• Tuchinda S., Beale D., Lehmann H. A new haemoglobin in a Thai family. A case of Haemoglobin Siriraj-β-Thalassaemia. Brit. Med. J. 1965; 1: 1583–1585
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Riggs A. Polymerization of hemoglobins of mouse and man. Structural basis. Science 1967; 158: 800–802
   PubMed Web of Science ®Google Scholar
• Arcasoy A., Casey R., Lehmann H., Cavdar A. O., Berki A. A new haemoglobin J from Turkey – Hb Ankara (β10 (A7) Ala→Asp). FEBS Letters 1974; 42: 121–123
   PubMed Web of Science ®Google Scholar
• Monn E., Gaffney P. J., Lehmann H. Hemoglobin Sogn (β14 Arginine). A new haemoglobin variant. Scand. J. Haemat. 1968; 5: 353–360
   PubMedGoogle Scholar
• Beuzard Y., Basset P., Braconnier F., El Gammal H., Martin L., Oudard J. L., Thillet J. Haemoglobin Saki α2β2 14 Leu→Pro (A11) structure and function. Biochim. Biophys. Acta 1975; 393: 182–187
   PubMed Web of Science ®Google Scholar
• Milner P. F., Corley C. C., Pomeroy W. L., Wilson J. B., Gravely M., Huisman T. H.J. Thalassemia intermedia caused by heterozygosity for both β-thalassemia and Hemoglobin Saki (β14 (A11) Leu→Pro). Amer. J. Hemat. 1976; 1: 283–292
   PubMed Web of Science ®Google Scholar
• Kennedy C. C., Blundell G., Lorkin P. A., Lang A., Lehmann H. Haemoglobin Belfast 15(A12) Tryptophan→Arginine: A new unstable haemoglobin variant. Brit. Med. J. 1974; 4: 324–326
   PubMed Web of Science ®Google Scholar
• 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 Haemat. 1976; 55: 313–319
   PubMed Web of Science ®Google Scholar
• Baglioni C., Weatherall D. J. Abnormal Human Hemoglobins IX. Chemistry of Hemoglobin J Baltimore. Biochim. Biophys. Acta 1963; 78: 637–643
   PubMed Web of Science ®Google Scholar
• Weatherall D. J. Hemoglobin J (Baltimore) Coexisting in a Family with Hemoglobin. S. Johns Hopkins Hosp. Bull. 1964; 114: 1–12
   PubMedGoogle Scholar
• Chernoff A. I., Perillie P. E. The amino acid composition of HGB New Haven #2 (HGB N New Haven). Biochim. Biophys. Res. Comm. 1964; 16: 368–372
   PubMed Web of Science ®Google Scholar
• Wong S. C., Bouver N., Wilson J. B., Huisman T. H.J. Hb J Georgia=Hb J Baltimore=α2β2 16Gly→Asp. Clin. Chim Acta 1971; 35: 521–522
   PubMed Web of Science ®Google Scholar
• Wade P. T., Jenkins T., Huehns E. R. Haemoglobin variant in a Bushman: Haemoglobin D β Bushman α β22 16Gly→Arg. Nature, London 1967; 216: 688–690
   PubMed Web of Science ®Google Scholar
• Maekawa M., Maekawa T., Fujiwara N., Tabara K., Matsuda G. Hemoglobin Nagasaki: αA2β2 17 Glu. A new abnormal human hemoglobin found in one family in Nagasaki. Int. J. Protein Research 1970; 11: 147–156
   Google Scholar
• Elion J., Belkhodja O., Wajcman H., Labie D. Two variants of Hemoglobin D in the Algerian population: Hemoglobin D Ouled Rabah β19(B1) Asn→Lys and Hemoglobin D Iran β22 (B4) Glu→Gln. Biochim. Biophys. Acta 1973; 310: 360–364
   PubMed Web of Science ®Google Scholar
• Lam H., Wilson J. B., Harris H., Gravely M., Huisman T. H.J. Hemoglobin Alamo [α2β2 19 (B1) Asn→Asp]. Hemoglobin 1977; 1: 703–706
   PubMed Web of Science ®Google Scholar
• Stamatoyannopoulos G., Nute P. E., Adamson J. W., Bellingham A. J., Funk D., Hornung S. Hemoglobin Olympia (β20 Valine→Wethionine): An electrophoretically silent variant associated with high oxygen affinity and erythrocytosis. J. Clin. Invest. 1973; 52: 342–349
   PubMed Web of Science ®Google Scholar
• Vella F., Lorkin P. A., Carrell R. W., Lehmann H. A new hemoglobin variant resembling Hemoglobin E. Hemoglobin E Saskatoon: β22 Glu→Lys. Canad. J. Biochem. 1967; 45: 1385–1391
   PubMedGoogle Scholar
• Blackwell R. Q., Yang H. J., Wang C. C. Henoglobin G Taipei: α2β2 22 Glu→Gly. Biochim. Biophys. Acta 1969; 175: 237–241
   PubMed Web of Science ®Google Scholar
• Vella F., Isaacs W. A., Lehmann H. Hemoglobin G Saskatoon: β22 Glu→Ala. Canad. J. Biochem. 1967; 45: 551–353
   PubMedGoogle Scholar
• Blackwell R. Q., Liu C. S., Yang H. J., Wang C. C., Huang J. T.H. Hemoglobin variant common to Chinese and North American Indians: α2β2 22 Glu→Ala. Science 1968; 161: 381–382
   PubMed Web of Science ®Google Scholar
• Bowman B. H., Barnett D. R., Hite R. Hemoglobin G Coushatta: a beta variant with a delta-like substitution. Biochem. Biophys. Res. Comm. 1967; 26: 466–470
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Ro I. H., Liu C. S., Yang H. J., Wang C. C., Huang J. T.H. Hemoglobin variant found in Koreans, Chinese, and North American Indians. α2β2 22 Glu→Ala. Am J. Phys. Anthrop. 1967; 30: 389–392
   Google Scholar
• Rahbar S. Haemoglobin D Iran: β22 Glutamic acid-Glu→amine (B4). Brit. J. Haemat. 1973; 24: 31–35
   PubMed Web of Science ®Google Scholar
• Garel M. C., Blouquit Y., Arous N., Rosa J. Hb Strasbourg α2β2 20(B2) Val→Asp: A variant at the same locus as Hb Olympia β20 Val→Met. FEBS Letters 1976; 72: 1–4
   PubMed Web of Science ®Google Scholar
• Forget B. G. Nucleotide Sequence of Human β Globin Messenger RNA. Hemoglobin 1977; 1: 879–881
   PubMed Web of Science ®Google Scholar
• Ranney H. M., Jacobs A. S., Udem L., ZaXusky R. Hemoglobin Riverdale-Bronx, an unstable hemoglobin resulting from the substitution of arginine for glycine at helical reside B6 of the β polypeptide chain. Biochim. Biophys. Acta 1968; 33: 1004–1011
   Google Scholar
• Huisman T. H.J., Brown A. K., Efremov G. D., Wilson J. B., Reynolds C. A., Uy R., Smith L. L. Hemoglobin Savannah (B6(24)β-Glycine→Valine): An unstable variant causing anemia with inclusion bodies. J. Clin. Invest. 1971; 50: 650–659
   PubMed Web of Science ®Google Scholar
• Idelson L. I., Didkowsky N. A., Casey R., Lorkin P. A., Lehmann H. New unstable haemoglobin (Hb Moscva, β24(B6) Gly→Asp) found in the U.S.S.R. Nature 1974; 249: 768–770
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C.-S. Hemoglobin G Taiwan-Ami α2β2 25 Gly→Arg. Biochim. Biophys. Res. Comm. 1968; 30: 690–696
   PubMed Web of Science ®Google Scholar
• Hunt J. A., Ingram V. M. Abnormal Human Haemoglobins VI. the chemical difference between haemoglobins A and E. Biochim. Biophys. Acta 1961; 49: 520–536
   PubMed Web of Science ®Google Scholar
• Blouquit Y., Arous N., Machado P. E.A., Garel M. C. Hb Henri Mondor: β26(B8) Glu→Val: A variant with a Substitution localized at the same position as that of Hb E β26 Glu→Lys. FEBS Letters 1976; 72: 5–7
   PubMed Web of Science ®Google Scholar
• Idelson L. I., Didkovsky N. A., Filippova A. V., Casey R., Kynoch P. A.M., Lehmann H. Haemoglobin Volga, β27 (B9) Ala→Asp, a new highly unstable haemoglobin with a suppressed charge. FEBS Letters 1975; 58: 122–125
   PubMed Web of Science ®Google Scholar
• Kuis-Reerink J. D., Jonxis J. H.P., Niazi G. A., Wilson J. B., Bolch K. C., Gravely M., Huisman T. H.J. Hb Volga or α2β2 27(B9) Ala→Asp: An unstable hemoglobin variant in three generations of a Dutch Family. Biochim. Biophys. Acta 1976; 439: 63–69
   PubMed Web of Science ®Google Scholar
• Cohen-Solal M., Seligmann M., Thillet J., Rosa J. Haemoglobin Saint Louis β28(B10) Leucine→Glutamine. A new unstable haemoglobin only present in a ferri form. Abstract 408, XIV int. Congress Hemat. San Paulo, 1972. FEBS Letters 1973; 33: 37–41
   PubMed Web of Science ®Google Scholar
• Thillet J., Cohen-Solal M., Seligmann M., Rosa J. Functional and physicochemical studies of Hemoglobin St. Louis β28 (B10) Leu→Gln. Journal of Clin. Invest. 1976; 58: 1098–1106
   PubMed Web of Science ®Google Scholar
• Sansone G., Carrell R. W., Lehmann H. Haemoglobin Genova: β28 (B10) Leucines→Proline. Nature, London 1967; 214: 877–879
   PubMed Web of Science ®Google Scholar
• Schmidt B., Bechtel K. C., Johnson M. H., Therrell B. J., Jr., Moo-Penn W. F. Hemoglobin Lufkin: β29 (B11) Gly→Asp: An unstable hemoglobin variant involving an internal amino acid residue. Hemoglobin 1977; 1: 700–814
   Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Baur E. W., Motulsky A. G. Structural characterization of Hemoglobin Tacoma. Biochemistry 1969; 8: 2125–2129
   PubMed Web of Science ®Google Scholar
• Jackson J. M., Yates A., Huehns E. R. Haemoglobin Perth: β32 (B14) Leu→Pro. An unstable haemoglobin causing haemolysis. Brit. J. Haemat. 1973; 25: 607–610
   PubMed Web of Science ®Google Scholar
• Honig G. R., Green D., Shamsuddin M., Vida L. N., Mason R. G., Gnarra D. J., Maurer H. S. Hemoglobin Abraham Lincoln, β32(B14) Leucine→Proline. An unstable variant producing severe hemolytic disease. J. Clin. Invest. 1973; 52: 1746–1755
   PubMed Web of Science ®Google Scholar
• Garel M. C., Blouquit Y., Rosa J. Hemoglobin Castilla β32(B14) Leu→Arg: A new unstable variant producing severe hemolytic disease. FEBS Letter 1975; 58: 145–147
   Web of Science ®Google Scholar
• Rieder R. F., Oski F. A., Clegg J. B. Hemoglobin Philly (β35 Tyrosiner→Phenylalanine): Studies in the molecular pathology of hemoglobin. J. Clin. Invest. 1969; 48: 1627–1642
   PubMed Web of Science ®Google Scholar
• Yamaoka K. Hemoglobin Hirose: α2β2 37(C5) Tryptophan yielding Serine. Blood 1971; 38: 730–738
   PubMed Web of Science ®Google Scholar
• Gacon G., Belkhodja O., Wajcman H., Labie D. Structural and Functional Studies of Hb Rothchild β37 (C3) Trp→Arg. A new variant of the α1β2 contact. FEBS Letters 1977; 82: 243–246
   PubMed Web of Science ®Google Scholar
• Brimhall B., Jones R. T., Schneider R. G., Hosty T. S., Tomlin G., Atkins R. Two new hemoglobins: Hemoglobin Alabama (β39 (C5) Gln→Lys) and Hemoglobin Montgomery (α48(CD6) Leu→Arg). Biochia. Biophys. Acta 1975; 379: 28–32
   PubMed Web of Science ®Google Scholar
• Kendall A. G., Pas A. T., Wilson B. J., Cope N., Bolch K., Huisman T. H.J. Hb Vaasa or α2β2 (39(C5) Gln→Glu), a mildly unstable variant found in a Finnish Family. Hemoglobin 1977; 1: 292–295
   PubMed Web of Science ®Google Scholar
• Brown W. J., Niazi G. A., Jayalakshmi M., Abraham E. C., Huisman T. H.J. Hemoglobin Athens-Georgia, or α2β2 40(C6) Arg→Lys, a hemoglobin variant with an increased oxygen affinity. Biochim. Biophys. Acta 1976; 439: 70–76
   PubMed Web of Science ®Google Scholar
• Moo-Penn W. F., Johnson M. H., Bechtel K. C., Jue D. L., Therrell B. L., Schmidt R. M. Hemoglobin Austin and Waco: two hemoglobins with substitutions in the α2β2 contact region. Archives of Biochemistry and Biophysics 1977; 179: 86–94
   PubMed Web of Science ®Google Scholar
• Burkett L. B., Sharma V. S., Pisciotta A. V., Ranney H. M., Bruckheimer S. Hemoglobin Mequon β41 (C7) Phenylalanine→Tyrosine. Blood 1976; 48: 645–651
   PubMed Web of Science ®Google Scholar
• Dacie J. V., Shinton N. K., Gaffney P. J., Jr., Carrell R. W., Lehmann H. Haemoglobin Hammersmith (β42(CD1) Phe→Ser). Nature, London 1967; 216: 663–665
   PubMed Web of Science ®Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Yamaguchi K., Yoneaitsu H., Ishii T., Shibata S. Hemoglobin Chiba: Hb Hammersmith in a Japanese Girl. Acta Haemat. Jap. 1975; 38: 53–58
   PubMedGoogle Scholar
• Keeling M. M., Ogdon L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitchens J. L., Huisman T. H.J. Hemoglobin Louisville (β42(CD1)Phe→Leu): An unstable variant causing mild hemolytic anemia. J. Clin. Invest. 1971; 50: 2395–2402
   PubMed Web of Science ®Google Scholar
• Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemoglobin Bucuresti β42(CD1) Phe→Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. Biophys. Acta 1971; 251: 1–6
   PubMed Web of Science ®Google Scholar
• Bowman B. H., Oliver C. P., Barnett D. R., Cunninghan J. R., Schneider R. G. Chemical characterization of three Hemoglobins G. Blood 1964; 23: 193–199
   Web of Science ®Google Scholar
• Allan N., Beale D., Irvine D., Lehmann H. Three haemoglobins K: Woolwich, an abnormal, Cameroon and Ibadan, two unusual variants of human Haemoglobin A. Nature, London 1965; 208: 658–661
   Web of Science ®Google Scholar
• Sick K., Beale D., Irvine D., Lehmann H., Goodall P. T., MacDougall S. Haemoglobin G Copenhagen and Haemoglobin J Cambridge. Two new β-chain variants of Haemoglobin A. Biochim. Biophys. Acta 1967; 140: 231–242
   PubMed Web of Science ®Google Scholar
• Marinucci M., Mavilio F., Tentori L., Alberti R. Hemoglobin Gavello α2β2 47(CD6) Asp→Gly, a new hemoglobin variant from Polesine (Italy). Hemoglobin 1977; 1: 771–779
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Milner P., Cobb L. Hemoglobin Okaloosa (β48(CD7) Leucine→Arginine. An unstable hemoglobin with decreased oxygen affinity. J. Clin. Invest. 1973; 52: 2858–2864
   PubMed Web of Science ®Google Scholar
• Labossiere A., Hill J. R., Vella F. A new βTp V Hemoglobin variant: Hb Edmonton. Clin. Biochem. 1971; 4: 114–117
   PubMed Web of Science ®Google Scholar
• Jones R. T., Koler R. D., Duerst M. L., Dhindsa D. S. Hemoglobin Willamette [α2β2 51 Pro→Arg (D2)] a new-abnormal human hemoglobin. Hemoglobin 1976; 1: 45–57
   PubMed Web of Science ®Google Scholar
• Konotey-Ahulu F. I.D., Kinderlerer J. L., Lehmann H., Ringelhann B. Haemoglobin Osu-Christiansborg: A new β-chain variant of Haemoglobin A (β52 (D3) Aspartic acid→Asparagine) in combination with Haemoglobin S. J. Med. Genet. 1971; 8: 302–305
   PubMed Web of Science ®Google Scholar
• Beresford C. H., Clegg J. B., Weatherall D. J. Haemoglobin Ocho Rios (β52(D3) Aspartic acid→Alanine); A new β-chain variant of Haemoglobin A found in combination with Haemoglobin S. J. Med. Genet. 1972; 9: 151–153
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. Abnormal Human Haemoglobins. Separation and Characterisation of the α and β chains by Chromatography, and the determination of two new variants. J. Mol. Biol. 1966; 19: 91–108
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C.-S. The identical structural anomalies of Hemoglobins J Meinung and J Korat. Biochem. Biophys. Res. Comm. 1966; 24: 732–738
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C.-S., Lie-Injo L. E., Pribadi W. Fast hemoglobin variant in Minahassan people of Sulawesi, Chinese and Thais: α2β2 56 Gly→Asp. An J. Phys. Anthrop 1970; 32: 147–150
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nowzari G., Haydari H., Daneshmand P. Haemoglobin Haraadan α2Aβ2 56 Glycine→Arginine (D7). Biochim. Biophys. Acta 1975; 379: 645–648
   PubMed Web of Science ®Google Scholar
• Giardina B., Brunori M., Antonini E., Tentori L. Properties of Hemoglobin G Ferrara (β57(E1) Asn→Lys). Biochim. Biophys. Acta 1978; 534: 1–6
   PubMed Web of Science ®Google Scholar
• Marengo-Rowe A. J., Lorkin P. A., Gallo E., Lehmann H. Haemoglobin Dhofar – a new variant from Southern Arabia. Biochim. Biophys. Acta 1968; 168: 58–63
   PubMed Web of Science ®Google Scholar
• Boulton F. E., Huntsman R. G., Lehmann H., Lorkin P., Romero Herrera A. Myoglobin variants. Brit. J. Haemat. 1971; 20: 671–672
   Web of Science ®Google Scholar
• Blackwell R. Q., Liu C.-S., Shih T.-B. Hemoglobin J Kaohsiung: β59 Lys→Thr. Biochim. Biophys. Acta 1971; 229: 343–348
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Jim R. T.S., Liu C.-S., Weng M.-I., Wang C.-L., Shih T.-B. Fast haemoglobin variant found in Hawaiian-Chinese-Caucasian family in Hawaii and a Chinese subject in Taiwan. Vox Sang. 1972; 22: 469–473
   PubMed Web of Science ®Google Scholar
• Wajcman H., Amegnizin K. P.E., Belkhodja O., Labie D. Hemoglobin J Lome β59(E3) Lys→Asn. A new fast moving variant found in a Togolese. FEBS Letters 1977; 84: 572–374
   Web of Science ®Google Scholar
• Kagimoto T., Morino Y., Kishimoto S. A new hemoglobin variant Hb Yatsushiro α2Aβ260 Val→Leu. Biochim. Biophys. Acta 1978; 532: 195–198
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huehns E. R., Motulsky A. G. Structural characterization of Hemoglobin N Seattle: α2Aβ2 61 Lys→Glu. Biochim. Biophys. Acta 1968; 154: 278–283
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Iuchi I., Ueda S., Takeda I. Hemoglobin Hikari (α2Aβ2 61 AspNH2): A fast moving hemoglobin found in two unrelated Japanese families. Clin. Chim. Acta 1964; 10: 101–105
   PubMed Web of Science ®Google Scholar
• Beutler E., Lang A., Lehmann H. Hemoglobin Duarts: α2β2 62 (E6) Ala→Pro: A new unstable hemoglobin with increased oxygen affinity. Blood 1974; 43: 527–535
   PubMed Web of Science ®Google Scholar
• Muller C. J., Kingma S. Haemoglobin Zürich α2Aβ263 Arg. Biochim. Biophys. Acta 1961; 50: 595
   PubMed Web of Science ®Google Scholar
• Gerald P. S., Efron M. L. Chemical studies of several varieties of Hb M. Proc. Natl. Acad. Sci. 1961; 47: 1758–1767
   PubMed Web of Science ®Google Scholar
• Shibata S., Miyaji T., Iuchi I., Ueda S. A comparatively study of Hemoglobin M Iwate and Hemoglobin M Kurume by means of electrophoresis, chromatography and analysis of peptide chains. Acta Haemat. Jap. 1961; 24: 486–494
   PubMedGoogle Scholar
• Murawski K., Szymanowska Z., Kozlowska J. A new variant of abnormal methaemoglobin: Hb M Radom. Biochim. Biophys. Acta 1963; 69: 442–444
   Web of Science ®Google Scholar
• Hobolth N. Haemoglobin M Arhus: I. Clinical family study. Acta Paediatrica Scandinavica 1965; 54: 357–362
   Web of Science ®Google Scholar
• Josephson A. M., Weinstein H. G., Yakulis V. J., Singer L., Heller P. A new variant of Hemoglobin M disease: Hemoglobin M Chicago. J. Lab. & Clin. Med. 1962; 59: 918–925
   PubMed Web of Science ®Google Scholar
• Betke K., Gröschner E., Bock K. Properties of a further variant of Haemoglobin M. Nature 1960; 188: 864–865
   Web of Science ®Google Scholar
• Hörlein H., Weber G. Über chronishe familiäre methänoglobinämie und eine neue modifikation des methämoglobins. Deutsche Medizinische Wochenschrift 1948; 73: 476–478
   PubMedGoogle Scholar
• Efremov G. D., Huisman T. H.J., Stanulovic M., Zurovec M., Duma H., Wilson J. B., Jeremic V. Haemoglobin M Saskatoon and Haemoglobin M Hyde Park in two Yugoslavian Families. Scand. J. Haemat. 1974; 13: 48–60
   PubMedGoogle Scholar
• Kohne E., Grosze H. P., Versmold H., Kley H. P., Kleihauer E. Hb M Erlangen: α2β2 63 (E7) Tyr. Eine neue Mutation mit Hämolyse und Diaphorasemangel. Kinderheilk 1975; 120: 69–78
   PubMedGoogle Scholar
• Wajcman H., Krishnamoorthy R., Gacon G., Elion J., Allard C., Labie D. A new hemoglobin variant involving the distal histidine: Hb Bicetre (β63(E7) His→Pro). J. Mol. Mod. 1976; 1: 187–197
   Google Scholar
• Tentori L. Three examples of double heterozygosis betathalassemia and rare hemoglobin variants. International Symposium on Abnormal Hemoglobin and Thalassemia, IstanbulTurkey, 1974, Abstract 68
   Google Scholar
• Ricco G., Pich P. G., Mazza U., Rossi G., Ajmar F., Arese P., Gallo E. Hb J Sicilia: β65(E9) Lys→Asn, a beta homologue of Hb Zambia. FEBS Letters 1974; 39: 200–204
   PubMed Web of Science ®Google Scholar
• Garel M. C., Hassan W., Coquelet M. T., Goossens M., Rosa J. Hemoglobin J Cairo: β65(E9) Lys→Gln, a new hemoglobin variant discovered in an Egyptian family. Biochim. Biophys. Acta 1976; 420: 97–104
   PubMed Web of Science ®Google Scholar
• Rosa J., Labie D., Wajcman H., Boigne J. M., Cabannes R., Bierme R., Ruffie J. Haemoglobin I Toulouse: β66 (E10 Lys→Glu: a new abnormal haemoglobin with a mutation localized on the E10 porphyrin surrounding zone. Nature, London 1969; 223: 190–191
   PubMed Web of Science ®Google Scholar
• Steadman J. H., Yates A., Huehns E. R. Idiopathic Heinz Body Anaemia: Hb-Bristol (β67(E11) Val→Asp). Brit. J. Haemat. 1970; 18: 435–446
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Lorkin P. A., Raik E., Hunter E. Haemoglobin Sydney: β67(E11) Valine→Alanine: An emerging pattern of unstable haemoglobins. Nature, London 1967; 215: 626–628
   PubMed Web of Science ®Google Scholar
• Ohba Y., Hiyaji T., Matsuoka M., Sugiyama K., Suzuki T, Sugiura T. Hemoglobin Mizulo or beta 68(E12) Leucine→Proline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin 1977; 1: 467–477
   PubMed Web of Science ®Google Scholar
• Salomon H., Tatarski I., Dance N., Huehns E. P., Shooter E. M. A new hemoglobin variant found in a Beduin tribe: Hemoglobin “Rambam.”. Israel Journal of Med. Sci. 1965; I: 836–840
   Google Scholar
• Kurachi S., Hermodson M., Hornung S., Stamatoyannopoulos G. Structure of Haemoglobin Seattle. Nature, New Biology 1973; 243: 275–276
   PubMedGoogle Scholar
• Carrell R. W., Owen M. C. A new approach to haemoglobin variant identification. Haemoglobin Christchurch β71(E15) Phenylalanine→Serine. Biochim. Biophys. Acta 1971; 236: 507–511
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Pootrakul S., Gray G. Hemoglobin Vancouver [α2β2 73(E17) Asp→Tyr]: Its structure and function. Journal of Molecular Evolution 1976; 9: 37–44
   PubMed Web of Science ®Google Scholar
• Konotey-Ahulu F. I.D., Gallo E., Lehmann H., Ringelhann B. Haemoglobin Korle-Bu (β73 Aspartic acid→Asparagine) showing one of the two amino acid substitutions of Haemoglobin C Harlem. J. Med. Genet. 1968; 5: 107–111
   PubMedGoogle Scholar
• Bio-Doku F. S., Kinderlerer J., Lehmann H. Submitted to Atlas of Protein Sequence and Structure. 1972; 5: 73
   Google Scholar
• Schneider R. G., Hosty T. S., Tomlin G., Atkins R., Brirahall B., Jones R. T. Hb Mobile [α2β2 73(E17) Asp→Val]: A new variant. Biochem. Genet. 1975; 13: 411–415
   PubMed Web of Science ®Google Scholar
• Rieder R. F., Wolf D. J., Clegg J. B., Lee S. L. Rapid post-synthetic destruction of unstable Haemoglobin Bushwick. Nature 1975; 254: 725–727
   PubMed Web of Science ®Google Scholar
• White J. M., Brain M. C., Lorkin P. A., Lehmann H., Smith M. Mild “Unstable Haemoglobin Haemolytic Anaemia” caused by Haemoglobin Shepherds Bush (β74 (E18) Gly→Asp). Nature, London 1970; 225: 939–941
   PubMed Web of Science ®Google Scholar
• Hubbard M., Winton E. F., Lindeman J. G., Dessauer P. L., Wilson J. B., Wrightstone R. N., Huisraan T. H.J. Hemoglobin Atlanta or α2β2 75 Leu→Pro (E19): an unstable variant found in several members of a Caucasian family. Biochim. Biophys. Acta 1975; 386: 538–541
   PubMed Web of Science ®Google Scholar
• Romain P. L., Schwartz A. D., Shamsuddin M., Adams J. G., III, Mason R. G., Vida L. N., Honig G. R. Hemoglobin J Chicago (β76 (E20) Ala→Asp); A new hemoglobin variant resulting from a substitution of an external residue. Blood 1975; 45: 387–393
   PubMed Web of Science ®Google Scholar
• Rahbar S., Beale D., Isaacs W. A., Lehmann H. Abnormal Haemoglobins in Iran. Observation of a new variant -Haemoglobin J Iran (α2β2 77 His→Arg). Brit. Med. J. 1967; 1: 674–677
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Shih T.-B., Wang C.-L., Liu C.-S. Hemoglobin C-Hsi-Tsou: β79 Asp→Gly. Biochim. Biophys. Acta 1972; 257: 49–53
   PubMedGoogle Scholar
• Benesch R., Edilji R., Benesch R. E. Oxygenation properties of hemoglobin variants with substitutions near the polyphosphate binding site. Biochim. Biophys. Acta 1975; 395: 368
   Google Scholar
• Blackwell R. Q., Yang H. T., Wang C. C. Hemoglobin G Szuhu: β80 Asn→Lys. Biochim. Biophys. Acta 1969; 185: 59–64
   Google Scholar
• Imai K., Morimoto H., Kotani M., Shibata S., Miyaji T., Masutomo K. Studies on the function of abnormal hemoglobins II. Oxygen equilibrium of abnormal hemoglobins: Shimonoseki, Ube II, Hikari, Gifu, and Agenogi. Biochim. Biophys. Acta 1970; 200: 197–202
   PubMedGoogle Scholar
• Schneider R. G., Hettig R. A., Bilunos M., Brimhall B. Hemoglobin Baylor [α2β2 81 (EF5) Leu→Arg] -an unstable mutant with high oxygen affinity. Hemoglobin 1976; 1: 85–96
   PubMed Web of Science ®Google Scholar
• Moo-Penn W. F., Jue D. L., Bechtel K. C., Johnson M. H., Schmidt R. M., McCurdy P. R., Fox J., Bonaventura J., Sullivan B., Bonaventura C. Hemoglobin Providence. A human hemoglobin variant occurring in two forms in vivo. J. of Biol. Chem. 1976; 251: 7557–7562
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Bonaventura C., Sullivan B., Ferruzzi G., McCurdy P. R., Fox J., Moo-Penn W. F. Hemoglobin Providence. Functional consequences of two alterations of the 2, 3-diphosphoglycerate binding site at position β82. J. of Biol. Chem. 1976; 251: 7563–7571
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Stephens A. D., Beard M. E.J., Wrigley P. F.M., Adams L., Lehmann H. Haemoglobin Rahere (β82 Lys→Thr): A new high affinity haemoglobin associated with decreased 2,3-diphosphoglycerate binding and relative polycythaemia. Brit. Med. J. 1975; 4: 200–202
   PubMed Web of Science ®Google Scholar
• Ikkala E., Koskela J., Pikkarainon P., Rahiala E.-L., El-Hazmi M. A.F., Nagai K., Lang A., Lehmann H. Hb Helsinki: A variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (β82 [EF6] Lys→Met). Acta Haemat 1976; 56: 257–275
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Liu C.-S., Wang C.-L. Hemoglobin Ta-li: β83 Gly→Cys. Biochim. Biophys. Acta 1971; 243: 467–474
   PubMed Web of Science ®Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos (α2β2 83(EF7) Gly→Asp). A new hemoglobin (Hb) variant. Annual Meeting of the American Society of Hematology, Miami, 1972, Abstract 168
   Google Scholar
• Tatsis B., Sofroniadou K., Stergiopoulos C. I. Hemoglobin Pyrgos α2β2 83(EF7) Gly→Asp: A new hemoglobin variant in double heterozygosity with Hemoglobin S. Blood 1976; 47: 827–832
   PubMed Web of Science ®Google Scholar
• Bradley T. B., Wohl R. C., Murphy S. B., Oski F. A., Bunn H. F. Properties of Hemoglobin Bryn Mawr, β85 Phe→Ser, a new spontaneous mutation producing an unstable hemoglobin with high oxygen affinity. Annual Meeting of the American Society of Hematology. 1972, Abstract 40
   Google Scholar
• de Weinstein B. I., White J. M., Wiltshire B. G., Lehmann H. A new unstable haemoglobin: Hb Buenos Aires, β85(F1) Phe→Ser. Acta Haemat. 1973; 50: 357–363
   PubMed Web of Science ®Google Scholar
• Watson-Williams E. J., Beale D., Irvine D., Lehmann H. A new haemoglobin, D Ibadan (β87 Threonine→Lysine), producing no sickle cell Haemoglobin D disease with Haemoglobin S. Nature, London 1965; 205: 1273–1276
   PubMed Web of Science ®Google Scholar
• Hollender A., Lorkin P. A., Lehmann H., Svensson B. New unstable Haemoglobin Böras: β88(F4) Leucine→Arginine. Nature, London 1969; 222: 953–955
   PubMed Web of Science ®Google Scholar
• Opfell R. W., Lorkin P. A., Lehmann H. Hereditary non-spherocytic haemolytic anaemia with post-splenectomy inclusion bodies and pigmenturia caused by an unstable Haemoglobin Santa Ana -β88(F4) Leucine→Proline. J. Med. Genet. 1968; 5: 292–297
   PubMedGoogle Scholar
• Thillet J., Blouquit Y., Garel M. C., Dreyfus B., Reyes F., Cohen-Solal M., Beuzard Y., Rosa J. Hemoglobin Creteil β89(F5) Ser→Asn: High oxygen affinity variant of hemoglobin frozen in a quarternary R-structure. J. of Mol. Med. 1976; 1: 135–150
   Google Scholar
• Paniker N. V., Lin Kuang-Tzu Davis, Krantz S. K., Flexner J. M., Wasserman B. K., Puett D. Haemoglobin Vanderbilt (α2β2 89 Ser→Arg): A New Haemoglobin with High Oxygen Affinity and Compensatory Frythrocytosis. Brit. J. Haemat. 1978; 39: 249–258
   PubMed Web of Science ®Google Scholar
• Miyaji R., Suzuki H., Ohba Y., Shibata S. Hemoglobin Agenogi (α2β2 90 Lys), a slow-moving hemoglobin of a Japanese family resembling Hb-E. Clin. Chim. Acta 1966; 14: 624–629
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Satoshi U., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin Sabine. β91 (F7) Leu→Pro. An unstable variant causing severe anemia with inclusion bodies. New Eng. J. Med. 1969; 280: 739–745
   PubMed Web of Science ®Google Scholar
• Ahern E., Ahern C., Hilton T., Serjeant G. R., Serjeant B. E., Seakins M., Lang A., Middleton A., Lehnann H. Haemoglobin Caribbean β91(F7) Leu→Arg: A mildly unstable haemoglobin with low oxygen affinity. FEBS Letters 1976; 69: 99–102
   PubMed Web of Science ®Google Scholar
• Heller P., Coleman R. D., Yakulis V. Hemoglobin M Hyde Park: A new variant of abnormal methemoglobin. J. Clin. Invest. 1966; 45: 1021–1025
   Web of Science ®Google Scholar
• Shibata S., Yamamoto K., Ohba Y., Miyaji R., Karita K., Iuchi I. Hemoglobin M Akita disease. Acta Haemat. Jap. 1969; 32: 311–329
   PubMedGoogle Scholar
• Beuzard Y., Courvalin J. Cl, Cohen Solal M., Garel M. C., Rosa J., Brizard C. P., Gibaud A. Structural studies of Hemoglobin Saint Etienne β92(F8) His→Gln: A new abnormal hemoglobin with loss of β proximal histidine and absence of heme on the β chains. FEBS Letters 1972; 27: 76–80
   PubMed Web of Science ®Google Scholar
• Aksoy M., Erdem S., Efremov G. D., Wilson J. B., Huisnan T. H.J., Schroeder W. A., Shelton J. R., Shelton J. B., Ulitin O. N., Müftüglu A. Hemoglobin Istanbul: Substitution of Glutamine for Histidine in a proximal Histidine (F8(92)β). J. Clin. Invest. 1972; 51: 2580–2537
   Web of Science ®Google Scholar
• Adams J. G., III, Przywara K. P., Shamsuddin M., Heller P. Hemoglobin J Altgeld Gardens (β92(FS) His→Asp): A new hemoglobin variant involving a substitution of the proximal histidine. Amer. Soc. Hemat. 18th Annual Meeting Dallas, Texas, 1975
   Google Scholar
• Finney R., Casey R., Lchmann H., Walker K. Hb Newcastle: β92(F8) His→Pro. FEBS Letters 1975; 60: 435–458
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Naughton M. A., Weatherall D. J. An improved method for the characterization of human haemoglobin mutants: Identification of α2β2 95 Glu, Haemoglobin N (Baltimore). Nature, London 1965; 207: 945–947
   PubMed Web of Science ®Google Scholar
• Gottlieb A. J., Robinson E. A., Itano H. A. Primary structure of Hopkins-I Haemoglobin. Nature 1967; 214: 189–190
   PubMed Web of Science ®Google Scholar
• Dobbs N. B., Jr., Simmons J. W., Wilson J. B., Huisman T. H.J. Hemoglobin Jenkins or Hemoglobin-N-Baltimore or α2β2 95 Glu. Biochim. Biophys. Acta 1966; 117: 492–494
   PubMed Web of Science ®Google Scholar
• Bayrakci C., Josephson A., Singer L., Heller P., Coleman R. D. A new fast hemoglobin. Xth Congress of the International Society of Haematology, StockholmSweden, 1964
   Google Scholar
• Hamilton H. H., Iuchi I., Miyaji T., Shibata S. Hemoglobin Hiroshima (β143 Histidine→Aspartic Acid): A newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia. (Personal communication P. Heller). J. Clin. Invest. 1969; 48: 525–535
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Lehmann H., Fairbanks V. F., Berglund G., Leonhardt T. Two new pathological haemoglobins: Olmsted β141 (H19) Leu→Arg and Malmö: β97(FG4) His→Gln. Biochem. J. 1970; 119: 68–74
   Web of Science ®Google Scholar
• Taketa F., Huang Y. P., Libnoch J. A., Dessel B. H. Hemoglobin Wood β97(FG4) His→Leu: A new high-oxygen-affinity hemoglobin associated with familial erythrocytosis. Biochim. Biophys. Acta 1975; 400: 348–353
   PubMed Web of Science ®Google Scholar
• Taketa F., Antholine W. E., Mauk A. G., Libnoch J. A. Nitrosylhemoglobin Wood: Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum. Biochemistry 1975; 14: 3229–3233
   PubMed Web of Science ®Google Scholar
• Carrell R. W., Lehmann H., Hutchison H. E. Haemoglobin Köln (β98 Valine→Methionine): An unstable protein causing inclusion-body anaemia. Nature, London 1966; 210: 915–916
   PubMed Web of Science ®Google Scholar
• Woodson R. D., Heywood J. D., Lenfant C. Oxygen transport in Hemoglobin San Francisco. Clin. Res. 1970; 18: 134
   Google Scholar
• Ohba Y., Hiyaji T., Shibata S. Identical substitution in Hb Ube-1 and Hb Köln. Nature, New. Biology 1973; 243: 205–207
   PubMedGoogle Scholar
• Gordon-Smith E. C., Dacie J. V., Blecher T. E., French E. A., Wiltshire B. G., Lehmann H. Haemoglobin Nottingham, β98 (FG5) Val→Gly: A new unstable haemoglobin producing severe haemolysis. Proc. Royal Soc. Med. 1973; 66: 507–508
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. A new unstable hemoglobin mutated in β98(FG5) Val→Ala: Hb Djelfa. FEBS Letters 1975; 58: 238–240
   PubMed Web of Science ®Google Scholar
• Reed C. S., Hampson R., Gordon S., Jones R. T., Novy H. 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
   PubMed Web of Science ®Google Scholar
• Jones R. T., Osgood E. E., Brimhall B., Koler R. D. Hemoglobin Yakima: I. Clinical and biochemical studies. J. Clin. Invest. 1967; 46: 1840–1847
   PubMed Web of Science ®Google Scholar
• Weatherall D. J., Clegg J. B., Callender S. T., Wells R. M.G., Gale R. E., Huehns E. R., Perutz M. F., Viggiano G., Ho C. Haemoglobin Radcliffe (α2β2 99(G1)Ala): A high oxygen-affinity variant causing familial polycythaenia. Britich Journal of Haematology 1977; 35: 177–191
   PubMed Web of Science ®Google Scholar
• Rucknagel D. L., Glynn K. P., Smith J. R. Hemoglobin Ypsilanti characterized by increased oxygen affinity, abnormal polymerization and erythremia. Clin. Res. 1967; 15: 270
   Google Scholar
• Lokich J. J., Mahoney C. W., Bunn H. F., Bruckheimer S. M., Ranney H. H. Hemoglobin Brigham (α2Aβ2 100 Pro→Leu). Hemoglobin variant associated v;ith familial erythrocytosis. J. Clin. Invest. 1975; 52: 2060–2067
   Google Scholar
• Jones R. T., Brimhall B., Gray G. Hemoglobin British Columbia [α2β2 101 (G3) Glu→Lys]: A new variant with high oxygen affinity. Hemoglobin 1976; 1: 171–182
   PubMed Web of Science ®Google Scholar
• Adams J. B., Winter W. P., Tausk K., Heller P. Hemoglobin Rush [(β-101(G3) Glutamine)]: A new unstable hemoglobin causing mild hemolytic anemia. Blood 1974; 45: 261–269
   Web of Science ®Google Scholar
• Mant M. J., Salkie M. L., Cope N., Appling F., Bolch K., Jayalakshmi M., Gravely M., Wilson J. B., Huisman T. H.J. Hb Alberta or α2β2 (101(G3) Glu→Gly), a new high-oxygen-affinity hemoglobin variant causing erythrocytosis. Hemoglobin 1976–77; 1: 183–194
   PubMed Web of Science ®Google Scholar
• Charache S., Jacobson R., Brimhall B., Murphy E. A., Hathaway P., Winslow R., Jones R., Rath C., Simkovich Joan. Hb Potomac (β101 Glu→Asp): Speculations on placental oxygen transport in carriers of high-affinity hemoglobins. Blood 1978; 51: 331–338
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Huisman T. H.J., Smith L. L., Wilson J. B., Kitchens J. L., Wrightstone R. N., Adams H. R. Hemoglobin Richmond, a human hemoglobin which forms asymmetric hybrids with other hemoglobins. J. Biol. Chera. 1969; 244: 6105–6116
   PubMed Web of Science ®Google Scholar
• Bonaventura J., Riggs A. Hemoglobin Kansas, a hunan hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. J. Biol. Chem. 1968; 243: 980–991
   PubMed Web of Science ®Google Scholar
• Nagel R. L., Joshua L., Johnson J., Landau L., Bookchin R. M., Harris M. B. Hemoglobin Beth Israel: A mutant causing clinically apparent cyanosis. New Eng. J. of Med. 1976; 295: 125–130
   PubMed Web of Science ®Google Scholar
• White J. M., Szur L., Gillies I. D.S., Lorkin P. A., Lehmann H. Familial polycythaemia caused by a new haemoglobin variant. Hb Heathrow β103(G5) Phenylalanine→Leucine. Brit. Med. J. 1973; 3: 665–667
   PubMed Web of Science ®Google Scholar
• Wilkinson T., Chua Ching Geh, Carrell R. W., Robin H., Exner T., Lee Kit Ming, Kronenberg H. A new haemoglobin variant, Haemoglobin Canperdown β104(G6) Arginine→Serine. Biochim. Biophvs. Acta 1975; 393: 195–200
   PubMed Web of Science ®Google Scholar
• Ryric D. R., Plowman D., Lehmann H. Haemoglobin Sherwood Forest β104(G6) Arg→Thr. FLBS Letters 1977; 83: 260–262
   PubMedGoogle Scholar
• Hyde R. D., Hall M. D., Wiltshire B. G., Lehnann H. Haemoglobin Southampton, β106(G8) Leu→Pro: An unstable variant producing severe haemolysis. Lancet 1972; 2: 1170–1172
   PubMed Web of Science ®Google Scholar
• Koler R. D., Jones R. T., Bigley R. H., Litt M., Lovrien E., Brooks R., Lahey M. E., Fowler R. Hemoglobin Casper: β106(G8) Leu→Pro, a contemporary mutation. Amer. J. Med. 1973; 55: 549–558
   PubMed Web of Science ®Google Scholar
• Kleihauer E., Waller H. D., Benöhr H. C., Kohne E., Gelinsky P. Hb Tübingen Eine neue β-Kettenvariante (βTp 10–12) mit erhöhter spontanozydation. Klin. Wschr. 1971; 48: 651–659
   Google Scholar
• Kohne E., Kley H. P., Kleihauer E., Versmold H., Benöhr H. C., Braunitzer G. Structural and functional characteristics of the Hb Tübingen:β106(G8) Leu→Gln. FEBS Letts. 1976; 64: 443–447
   PubMed Web of Science ®Google Scholar
• Jones R. T., Koler R. D. Functional studies of seven new abnormal hemoglobins. 16th International Congress in Hematology. September, 1976, Abstract No. 1–21.
   Google Scholar
• Imamura T., Fujita S., Ohta Y., Hanada M., Yanase T. Hemoglobin Yoshizuka (G10(108) β Asparagine→Aspartic acid): A new variant with a reduced oxygen affinity from a Japanese family. J. Clin. Invest. 1969; 48: 2341–2548
   PubMed Web of Science ®Google Scholar
• Nute P. E., Stamatoyannopoulos G., Hermodson M. A., Roth D., Hornung S. Hemoglobinopathic erythrocytosis due to a new electrophoretically silent variant, Hemoglobin San Diego (β109(G11) Val→Met). J. Clin. Invest. 1974; 53: 320–328
   PubMed Web of Science ®Google Scholar
• King M. A.R., Wiltshire B. G., Lehnann H., Morinoto H. An unstable haemoglobin with reduced oxygen affinity: Haemoglobin Peterborough, β111 (G13) Valines→Phenylalanine, its interaction with normal haemoglobin and with Haemoglobin Lepore. Brit. J. Haemat. 1972; 22: 125–134
   PubMed Web of Science ®Google Scholar
• Adams J. G., Boxer L. A., Baehner R. L., Forget B. G., Tsistrokis G. A., Steinberg M. H. Hemoglobin Indianapolis: Post-translational degradation of an unstable β-chain variant producing a phenotype of severe heterozygous β-Thalassemia. Clinical Research 1978; 26: 501A
   Google Scholar
• Ranney H. M., Jacobs A. S., Nagel R. L. Haemoglobin New York. Nature 1967; 213: 876–878
   PubMed Web of Science ®Google Scholar
• Outeirino J., Casey R., White J. M., Lehmann H. Haemoglobin Madrid, β115(G17) Alanine→Proline: An unstable variant associated with haemolytic anaemia. Acta Haemat. 1974; 52: 53–60
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Alperin J. B., Brimhall B., Jones R. T. Hemoglobin P(α2β2 117Arg): Structure and properties. J. Lab. Clin. Med. 1969; 73: 616–622
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Berkman N. L., Brimhall B., Jones R. T. Hemoglobin Fannin-Lubbock [α2β2119 (GH2) Gly→Asp]: A slightly unstable mutant. Biochim. Biophys. Acta 1976; 453: 478–483
   PubMed Web of Science ®Google Scholar
• Moo-Penn W. F., Bechtel K. C., Johnson M. H., Jue D. L., Therrell B. L., Jr., Morrison B. Y., Schmidt R. M. Hemoglobin Fannin-Lubbock [α2β2119 (GH2) Gly→Asp]: A new hemoglobin variant at the α1β1 contact. Biochim. Biophys. Acta 1976; 453: 472–477
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Hamilton H. B. Hemoglobin Hijiyama: A new fast-moving hemoglobin in a Japanese family. Science 1968; 159: 204–206
   PubMedGoogle Scholar
• El-Hazmi M. A.F., Lehmann H. Hemoglobin Riyadh [α2β2 120(GH3) Lys→Asn]-a new variant found in assocition with α-thalassemia and iron deficiency. Hemoglobin 1976; 1: 59–74
   PubMed Web of Science ®Google Scholar
• Miyaji T., Ohba Y., Matsuoka M., Kudoh H., Asano M., Yamamoto K., Satoh T. Hemoglobin Karatsu: Beta 120(GH3) Lysine→Asparagine. An example of Hb Riyadh in Japan. Hemoglobin 1977; 1: 461–466
   PubMed Web of Science ®Google Scholar
• Baglioni C. Abnormal Human Haemoglobins. VIII. Chemical studies on Haemoglobin D. Biochim. Biophys. Acta 1962; 59: 437–449
   PubMed Web of Science ®Google Scholar
• Ozsoylo S. Homozygous Hemoglobin D Punjab. Acta Haemat. 1970; 43: 353–359
   PubMed Web of Science ®Google Scholar
• Ramot B., Rotem J., Rahbar S., Jacobs A. S., Uden L., Ranney H. M. Hemoglobin D Punjab in a Bulgarian Jewish Family. Israel J. Med. Sci. 1969; 5: 1066–1070
   PubMedGoogle Scholar
• Smith E. W., Conley C. L. Sickle cell-hemoglobin D disease. Ann. Intern. Med. 1959; 50: 94–98
   PubMed Web of Science ®Google Scholar
• Wasi P., Pootrakul S., Na-Nakorn S., Beale D., Lehmann H. Haemoglobin D β Los Angeles (D Punjab, α2β2 121 Glu NH2) in a Thai Family. Acta Haemat. 1968; 39: 151–158
   PubMed Web of Science ®Google Scholar
• Imamura T., Riggs A. Identification of Hemoglobin Oak Ridge with Hemoglobin D Punjab (Los Angeles). Biochemical Genetics 1972; 7: 127–130
   PubMed Web of Science ®Google Scholar
• Bowman B., Ingram V. M. Abnormal human haemoglobins VII. the comparison of normal human haemoglobin D Chicago. Biochim. Biophys. Acta 1961; 53: 569–573
   PubMed Web of Science ®Google Scholar
• Baglioni C., Lehmann H. Chemical heterogeneity of Haemoglobin O. Nature 1962; 196: 229–232
   PubMed Web of Science ®Google Scholar
• Kamel K., Hoerman K., Awny A. Ethnological significance of hemoglobin α2β2 121 Lys. Am. J. Phys. Anthrop. 1970; 26: 107–108
   Web of Science ®Google Scholar
• Efremov G. D., Duma H., Ruvidic R., Rolovic Z., Wilson J. B., Huisman T. H.J. Hemoglobin Beograd or α2β2 121 Glu→Val (GH4). Biochim. Biophys. Acta 1973; 328: 81–83
   PubMed Web of Science ®Google Scholar
• Clegg J. B., Weatherall D. J., Boon Wong Hock, Mustafa D. Two new haemoglobin variants involving proline substitutions. Nature, London 1969; 22: 379–380
   Web of Science ®Google Scholar
• Miyagi T., Ohba Y., Yamamoto K., Shibata S., Iuchi I., Takenaka H. Japanese haemoglobin variant. Nature, London 1968; 217: 89–90
   Web of Science ®Google Scholar
• Altay C., Altinöz N., Wilson J. B., Bolch K. C., Huisman T. H.J. Hemoglobin Hacettepe or α2β2 127 (H5) Gln→Glu. Biochim. Biophys. Acta 1976; 434: 1–3
   PubMed Web of Science ®Google Scholar
• Martinez G., Lima F., Colombo B. Haemoglobin J Guantanamo (α2β2 128 (H6) Ala→Asp). A new fast unstable haemoglobin found in a Cuban Family. Biochim. Biophys. Acta 1977; 491: 1–6
   PubMed Web of Science ®Google Scholar
• Blackwell R. Q., Yang Y.-J., Wang C.-C. Hemoglobin J Taichung: β129 Ala→Asp. Biochim. Biophys. Acta 1969; 194: 1–5
   PubMed Web of Science ®Google Scholar
• Lorkin P. A., Pietschmann H., Braunsteiner H., Lehmann H. Structure of Haemoglobin Wien β130 (H8) Tyrosine→Aspartic acid: An unstable haemoglobin variant. Acta Haemat. 1974; 51: 351–361
   PubMed Web of Science ®Google Scholar
• WadeCohen P. T., Yates A., Bellingham A. J., Huehns E. R. Amino-acid substitution on the α1β1 intersubunit contact of Haemoglobin Camden β131 (H9) Gln→Glu. Nature, New Biology 1973; 245: 467–468
   Google Scholar
• Ohba Y., Miyaji T., Matsuoka M., Ueda S., Iuchi I., Shibata S. Hemoglobin Tokuchi: β131 Glutaaine→Glutamic acid, an example of Hb Camden in Japan. Acta Haemat. Jap. 1975; 38: 1–7
   PubMedGoogle Scholar
• Arends T., Lehmann H., Plowman D., Stathopoulou R. Haemoglobin North Shore-Caracas β134 (H12) Valines→Glutamic acid. FEBS Letters 1977; 80: 261–265
   PubMed Web of Science ®Google Scholar
• Brennan S. O., Arnold B., Fleming P., Carrell R. W. A new unstable haemoglobin, β134 Val→Glu. Proceedings New Zealand Medical Journal 1977; 85: 398
   Google Scholar
• Marti H. R., Winterhalter K. H., Di Iorio E. E., Lorkin P. A., Lehmann H. Hb Altdorf α2β2 135 (H13) Ala→Pro: A new electrophoretically silent unstable haemoglobin variant from Switzerland. FEBS Letters 1976; 63: 193–196
   PubMed Web of Science ®Google Scholar
• Minnich V., Hill R. J., Khuri P. D., Anderson M. E. Hemoglobin Hope: A beta chain variant. Blood 1965; 25: 830–838
   PubMed Web of Science ®Google Scholar
• Tentori L., Carta Sorcini M., Bucella C. Hemoglobin Abruzzo: Beta 143 (H21) His→Arg. Clin. Chim. Acta 1972; 38: 258–262
   PubMed Web of Science ®Google Scholar
• Bromberg P. A., Alben J. O., Bare G. H., Balcerzak S. P., Jones R. T., Brimhall B., Padilla F. Hemoglobin Little Rock (β143 His→Gln: (H21)). A high oxygen affinity haemoglobin variant with unique properties. Nature, New Biology 1973; 243: 177–179
   PubMedGoogle Scholar
• Jensen M., Oski F. A., Nathan D. G., Bunn H. F. Hemoglobin Syracuse (α2β2 143 (H21) His→Pro), a new high-affinity variant detected by special electrophoretic methods. J. Clin. Invest. 1975; 55: 469–477
   PubMed Web of Science ®Google Scholar
• Zak S. J., Brimhall B., Jones R. T., Kaplan M. E. Hemoglobin Andrew-Minneapolis α2Aβ2 144 Lys→Asn: A new high-oxygen-affinity mutant human hemoglobin. Blood 1974; 44: 543–549
   PubMed Web of Science ®Google Scholar
• Hayashim A., Stamatoyannopoulos G., Yoshida A., Adamson J. Haemoglobin Rainier: β145(HC2) Tyrosine→Cysteine and Haemoglobin Bethesda: β145 (HC2) Tyrosine→Histidine. Nature, New Biology 1971; 230: 264–267
   PubMedGoogle Scholar
• Kleckner H. B., Wilson J. B., Lindeman J. G., Stevens P. D., Niazi G., Hunter E., Chen C. J., Huisman T. H.J. Hemoglobin Fort Gordon or α2β2 145 Tyr→Asp, a new high-oxygen-affinity-hemoglobin variant. Biochim. Biophys. Acta 1975; 400: 343–347
   PubMed Web of Science ®Google Scholar
• Charache S., Brimhall B., Jones R. T. Polycythemia produced by Hemoglobin Osier (β145(HC2) Tyr→Asp). Johns Hopkins Med. J. 1975; 136: 132–156
   PubMedGoogle Scholar
• Gacon G., Wajcman H., Labie D. Structural and functional study of Hb Nancy β145 (HC2) Tyr→Asp: A high oxygen affinity hemoglobin. FEBS Letters 1975; 56: 39–42
   PubMedGoogle Scholar
• Winslow R. M., Swenberg M.-L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin McKees Rocks (α2β2 145 Tyr→Term): A human “nonsense” mutation leading to a shortened β-chain. J. Clin. Invest. 1976; 57: 772–781
   PubMed Web of Science ®Google Scholar
• Perutz M. F., del Pulsinelli P., Ten Eyck L., Kilnartin J. V., Shibata S., Iuchi I., Miyaji T., Hamilton H. B. Haemoglobin Hiroshima and the mechanisms of the alkaline Bohr affect. Nature, New Biology 1971; 252: 147–149
   Google Scholar
• Barera G. H., Bromberg P. A., Alben J. O., Brimhall B., Jones R. T., Mintz S., Rother I. Altered C-terminal salt bridges in Haemoglobin York cause high oxygen affinity. Nature 1976; 259: 155–156
   PubMed Web of Science ®Google Scholar
• Wajcman H., Kilmartin J. V., Najman A., Labie D. Hemoglobin Cochin-Port-Royal -consequences of the replacement of the β chain C-terminal by an arginine. Biochim. Biophys. Acta 1975; 400: 334–364
   PubMedGoogle Scholar
• Moo-Penn W. F., Wolff J. A., Simon G., Vaček M., Jue D. L., Johnson M. H. Hemoglobin Presbyterian: β108(G10) Asparagine→Lysine. A hemoglobin variant with low oxygen affinity. FEBS Letts. 1975; 92: 53–56
   Google Scholar
• Marinucci M., Mavilio F., Hassa A., Gabbianelli M., Tentori L., Ignesti C. Haemoglobin Prato: A new amino acid substitution (α31(B12) Arg→Ser). IRCS Medical Science 1978; 6: 234
   Google Scholar
• Honig G. R., Shamsuddin M., Tremaine L. M., Mason R. G., Vida L. N., Sarnwick R., Shahidi N. T. Hemoglobin Nigeria (α81 Ser→Cys), a new variant having an inhibitory effect on the gelation of sickle hemoglobin. Blood 1978; 52(supplement 1)113, no. 117
   Google Scholar
• Bursaux E., Blouquit Y., Poyart C., Rosa J., Arous N., Bohn B. Hemoglobin Ty Gard (α2Aβ2 124(H2) Pro→Gin) A stable high O2 affinity variant at the α1 β1, contact. FEBS Letters 1978; 88: 155–159
   PubMed Web of Science ®Google Scholar
• Moo-Penn W. F., Schneider R. G., Andrian S., Das D. K. Hemoglobin Detroit: β95 (FG2) Lysine→Asparagine. Biochim. Biophys. Acta 1978; 536: 283–288
   PubMed Web of Science ®Google Scholar
• Knuth A., Pribilla W., Marti H. R., Winterhalter K. H. Hemoglobin Moabit: Alpha 86 (F7) Leu→Arg. A New Unstable Abnormal Hemoglobin. Acta Haemat. 1979; 61: 121–124
   PubMed Web of Science ®Google Scholar
• Sanguansermsri T., Matragoon S., Changloah L., Flatz G. Hemoglobin Suan-Dok (α2 109 (G16) Leu→Arg β2): An Unstable Variant Associated with α-thalassemia. Hemoglobin 1979; 3: 161–174
   PubMed Web of Science ®Google Scholar
• Jue D. L., Johnson M. H., Patchen L. C., Moo-Penn K. F. Hemoglobin Dunn: α6 (A4) Aspartic Acid→Asparagine. Hemoglobin 1979; 3: 137–143
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Shelton J. B., Shelton J. R., Powars D. Hemoglobin Sunshine Seth -α2 (94(G1) Asp→His) β2. Hemoglobin 1979; 3: 145–159
   PubMed Web of Science ®Google Scholar
• Iuchi I., Ueda S., Hidaka K., Shibata S. Hemoglobin Hoshida (β43 (CD-2) Glu→Gin), A New Hemoglobin Variant Discovered in Japan. Hemoglobin 1978; 2: 235–247
   PubMed Web of Science ®Google Scholar
• Rahbar S., Nozari G., Ala F. Haemoglobin Avicenna (β47 (CD6) Asp→Ala), A New Abnormal Haemoglobin. Biochimica et Biophysica Acta 1979; 576: 466–470
   PubMed Web of Science ®Google Scholar
• Chen-Marotel J., Braconnier F., Blouquit Y., Martin-Caburi J., Kammerer J., Rosa J. Hemoglobin Bougardircy-Mali β119 (→2) Gly→Val. An Electrophoretically Silent Variant Migrating in Isoelectrofocusing as Hb F. Hemoglobin, 3, in press
   PubMedGoogle Scholar
• Omura H., Miyaji T., Shibata S. Hemoglobin F Ube (108 Asn→Lys), A New Abnormal Fetal Hemoglobin Found in a Japanese Baby. Chemical Abstracts 1975; 83: 266
   Google Scholar
• Maniatis A., Bousios T., Nagel R. L., Balazs T., Ueda Y., Bookchin R. M., Maniatis G. M. Hemoglobin Crete (β129 Ala→Pro): A New High-Affinity Variant Interacting with β°-and δβ°-Thalassemia. Blood 1979; 54: 54–63
   PubMed Web of Science ®Google Scholar