THREE NEW VARIANTS OF THE α1-GLOBIN GENE WITHOUT CLINICAL OR HEMATOLOGIC EFFECTS: Hb HAGERSTOWN [α44(CE2)Pro→Ala (α1)]; Hb BUFFALO [α89(FG1)His→Gln (α1)], A HEMOGLOBIN VARIANT FROM SOMALIA AND YEMEN; Hb WICHITA [α95(G2)Pro→Gln (α1)]; AND A SECOND, UNRELATED, CASE OF Hb ROUBAIX [α55(E4)Val→Leu (α1)]

REFERENCES

• Hojas-Bernal R., McNab-Martin P., Fairbanks V. F., Holmes M. W., Hoyer J. D., McCormick D. J., Kubik K. S. Hb Chile [β28(B10)Leu→Met]: An Unstable Hemoglobin Associated with Chronic Methemoglobinemia and Sulfonamide or Methylene Blue-Induced Hemolytic Anemia. Hemoglobin 1999; 23(2)125–134
   PubMed Web of Science ®Google Scholar
• Krishnan K., Martinez F., Wille R. T., Jones R. T., Shih D. T., Head C., Fairbanks V. F., Dabich L. Hb Washtenaw [β11(A8)Val→Phe]: An Electrophoretically Silent, Unstable, Low Oxygen Affinity Variant Associated with Anemia and Chronic Cyanosis. Hemoglobin 1994; 18 (4&5): 285–295
   Google Scholar
• Hutt P. J., Fairbanks V. F., Thibodeau S. N., Green M. M., Hoyer J. D., Block S. H., Day C., Jones R. T., Barwick R. C. Hb T-Cambodia, a β Chain Variant with the Mutations of Hb E and Hb D-Punjab, Confirmed by DNA Analysis. Hemoglobin 1997; 21(3)205–218
   PubMed Web of Science ®Google Scholar
• Schneider R. G., Barwick R. C. Measuring Relative Electrophoretic Mobilities of Mutant Hemoglobins and Globin Chains. Hemoglobin 1978; 2(5)417–435
   PubMed Web of Science ®Google Scholar
• Hocking D. R. The Separation and Identification of Hemoglobin Variants by Isoelectric Focusing Electrophoresis. An Interpretive Guide, T.H. J. Huisman. Isolab, Inc.:, Akron OHUSA 1997
   Google Scholar
• Honig G. R., Vida L. N., Shamsuddin M., Mason R. G., Schlumpf H. W., Luke R. A. Hemoglobin Milledgeville (α44 (CD2) Pro→Leu): a New Variant With Increased Oxygen Affinity. Biochim. Biophys. Acta 1980; 626(2)424–431
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ueda S., Shibata S., Imai K., Ohba Y., Shinohara T., Horio S., Nishioka K., Shirotani H. Hemoglobin Kawachi [α44 (CE2) Pro→Arg]: A New Hemoglobin Variant of High Oxygen Affinity with Amino Acid Substitution at α1β2 Contact. Hemoglobin 1982; 6(1)43–49
   PubMed Web of Science ®Google Scholar
• Williamson D., Langdown J. V., Myles T., Mason C., Henthorn J. S., Davies S. C. Polycythaemia and Microcytosis Arising from the Combination of a New High Oxygen Affinity Haemoglobin (Hb Luton, α89 His→Leu) and α Thalassaemia Trait. Br. J. Haematol. 1992; 82(3)621–622
   PubMedGoogle Scholar
• Déon C., Promé J. C., Promé D., Francina A., Groff P., Kalmes G., Galactéros F., Wajcman H. Combined Mass Spectrometric Methods for the Characterization of Human Hemoglobin Variants Localized within αT9 Peptide: Identification of Hb Villeurbanne α89 (FG1) His→Tyr. J. Mass Spectrom. 1997; 32(8)880–887
   PubMedGoogle Scholar
• Phillips S. E., Perutz M. F., Poyart C., Wajcman H. Structure and Function of Haemoglobin Barcelona Asp FG1(94) β to His. J. Molec. Biol. 1983; 164(3)477–480
   PubMedGoogle Scholar
• Como P. F., Kennett D., Wilkinson T., Kronenberg H. A New Hemoglobin with High Oxygen Affinity Hemoglobin Bunbury: α2β2 [94 (FG1) Asp→Asn]. Hemoglobin 1983; 7(5)413–421
   PubMed Web of Science ®Google Scholar
• Huisman T.H. J., Adams H. R., Wilson J. B., Efremov G. D., Reynolds C. A., Wrightstone R. N. Hemoglobin G Georgia or α295Leu(G-2)β2. Biochim. Biophys. Acta 1970; 200(3)578–580
   PubMedGoogle Scholar
• de Jong W.W. W., Bernini L. F., Meera Khan P. Haemoglobin Rampa: α95 Pro→Ser. Biochim. Biophys. Acta 1971; 236(1)197–200
   PubMedGoogle Scholar
• Smith L. L., Plese C. F., Barton B. P. Subunit Dissociation of the Abnormal Hemoglobins G Georgia (α2 95Leu (G2) β2) and Rampa (α2 95 Ser (G2) β2. J. Biol. Chem. 1972; 247: 1433–1439
   PubMed Web of Science ®Google Scholar
• Wiltshire B. G., Clark K. G., 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(3)459–464
   PubMedGoogle Scholar
• Lorkin P. A., Casey R., Clark K. G., Lehmann H. The Oxygen Affinity of Haemoglobin St. Luke's. 1974 39 (1); 111–114
   Google Scholar
• Bannister W. H., Grech J. L., Plese C. F., Smith L. L., Barton B. P., Wilson J. B., Reynolds C. A., Huisman T.H. J. Hemoglobin St Luke's, or α2 95 Arg (G2)β2. Eur. J. Biochem. 1972; 29(2)301–307
   PubMedGoogle Scholar
• Wajcman H., Kister J., Riou J., Galactéros F., Girot R., Maier-Redelsperger M., Nayudu N.V. S., Giordano P. C. Hb Godavari [α95(G2)Pro→Thr]: a Neutral Amino Acid Substitution in the α1β2 Interface That Modifies the Electrophoretic Mobility of Hemoglobin. Hemoglobin 1998; 22(1)11–22
   PubMed Web of Science ®Google Scholar
• Lokich J. J., Moloney C. W., Bunn H. F., Bruckheimer S. M., Ranney H. M. Hemoglobin Brigham (α2Aβ2 100 Pro→Leu). Hemoglobin Variant Associated with Familial Erythrocytosis. J. Clin. Invest. 1973; 52(8)2060–2067
   PubMed Web of Science ®Google Scholar
• 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. Biochim. Biophys. Acta 1985; 832(2)192–196
   PubMedGoogle Scholar
• Préhu C., Bost M., Barro C., Prome D., Riou J., Godart C., Kister J., Galactéros F., Wajcman H. Hb Roubaix [α55(E4)Val→Leu]: a New Neutral Hemoglobin Variant Involving the α1 Gene. Hemoglobin 1999; 23(4)361–365
   PubMed 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(1)195–198
   PubMedGoogle Scholar
• Williamson D., Brennan S. O., Muir H., Carrell R. W. Hemoglobin Collingwood β60 (E4) Val→Ala–A New Unstable Hemoglobin. Hemoglobin 1983; 7(6)511–519
   PubMed Web of Science ®Google Scholar
• Podda A., Galanello R., Maccioni L., Melis M. A., Rosatelli C., Perseu L., Cao A. Hemoglobin Cagliari (β60[E4]Val→Glu): a Novel Unstable Thalassemic Hemoglobinopathy. Blood 1999; 77(2)371–375
   Google Scholar