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Hemoglobin
international journal for hemoglobin research
Volume 1, 1976 - Issue 2
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Original Article

Hb-Alberta or α2β2 (101(G3) GLU→GLY), a New High-Oxygen-Affinity Hemoglobin Variant Causing Erythrocytosis

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Pages 183-194 | Published online: 07 Jul 2009

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Read on this site (21)

M. F. H. Carver & T. H. J. Huisman. (1997) International Hemoglobin Information Center Variant List. Hemoglobin 21:6, pages 505-506.
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. (1996) Variants of the Alpha Chain. Hemoglobin 20:3, pages 215-312.
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. (1994) International Hemoglobin Information Center. Hemoglobin 18:2, pages 77-161.
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. (1993) Variants of the Alpea Chain. Hemoglobin 17:2, pages 89-177.
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. (1992) Variants of the Alpha Chain. Hemoglobin 16:3, pages 127-213.
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. (1990) International Hemoglobin Information Center. Hemoglobin 14:3, pages 249-325.
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. (1989) Variants of the Alpha Chain. Hemoglobin 13:3, pages 223-297.
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. (1988) IHIC Variants List. Hemoglobin 12:3, pages 209-282.
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M. A. M. Ali, P. Pinkerton, S. W. S. Chow, S. D. Zaetz, J. B. Wilson, B. B. Webber, H. Hu, F. Kutlar & T. H. J. Huisman. (1988) Some Rare Hemoglobin Variants with Altered Oxygen Affinities; Hb Linkoping [β36(C2)Pro→Thr], Hb Caribbean [β91(F7)Leu→Ar6], and Hb Sunnybrook [β 36(C2)Pro→Arg]. Hemoglobin 12:2, pages 137-148.
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. (1987) IHIC Variants List. Hemoglobin 11:3, pages 243-308.
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. (1985) International Hemoglobin Information Center. Hemoglobin 9:3, pages 229-298.
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R. T. Jones & T.-B. Shih. (1980) Hemoglobin Variants with Altered Oxygen Affinity. Hemoglobin 4:3-4, pages 243-261.
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. (1978) Variant Lists. Hemoglobin 2:6, pages 567-598.
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S. C. Wong, M. A. R. Ali, W. Nicholson, J. B. Wilson, H. Lam & T. N. J. Huisman. (1978) A Second Patient with Hemoglobin Alberta, a High-Oxygen-Affinity Variant Causing Erythrocytosis and Forming Asymmetric Tetramers. Hemoglobin 2:6, pages 557-559.
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. (1977) International Hemoglobin Information Center. Hemoglobin 1:7, pages 707-733.
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Articles from other publishers (9)

Yue Yuan, Catherine Byrd, Tong-Jian Shen, Virgil Simplaceanu, Tsuey Chyi S. Tam & Chien Ho. (2013) Role of β/δ101Gln in Regulating the Effect of Temperature and Allosteric Effectors on Oxygen Affinity in Woolly Mammoth Hemoglobin. Biochemistry 52:49, pages 8888-8897.
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Marcilene Rezende Silva, Shimene Mascarenhas Sendin, Cibele Velloso-Rodrigues, André Rolim Belisário, Terezinha Santos D’Ávila, Liege Ribeiro Lyra & Marcos Borato Viana. (2012) Unstable hemoglobin Rush [beta 101(G3) Glu>Gln, HBB:c.304G>C] in a Brazilian family with moderate hemolytic anemia. Annals of Hematology 91:7, pages 1091-1096.
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R Chatterjee, E V Welty, R Y Walder, S L Pruitt, P H Rogers, A Arnone & J A Walder. (1986) Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1----lysine 99 alpha 2).. Journal of Biological Chemistry 261:21, pages 9929-9937.
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D T Shih, R T Jones, K Imai & I Tyuma. (1985) Involvement of Glu G3(101)beta in the function of hemoglobin. Comparative O2 equilibrium studies of human mutant hemoglobins.. Journal of Biological Chemistry 260:10, pages 5919-5924.
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Melisenda J. McDonald, Susan M. Turci, Margaret Bleichman & Robert A. Stinson. (1985) Functional and subunit assembly properties of hemoglobin alberta (α2β2101 Glu → Gly). Journal of Molecular Biology 183:1, pages 105-112.
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T. Nakatsuji, K. Shimizu & T.H.J. Huisman. (1984) Hb F-LA grange or α2γ2101(G3)Glu → Lys; 75IIe; 136Gly: A high affinity fetal hemoglobin variant observed in a caucasian newborn. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 789:2, pages 224-228.
Crossref
C.A. Harasym & R.A. Stinson. (1980) Asymmetric hybrids between hemoglobin alberta (α2β2 101 Glu→Gly) and hemoglobins A, A2 or FI in different liganded states. Clinical Biochemistry 13:2, pages 95-98.
Crossref
M. E. J. Beard, J. W. Hamer, S. O. Brennan, J. N. Jones, J. M. Sheat & J. S. Maclaurin. (2008) Familial Relative Polycythaemia due to Haemoglobin Heathrow. Australian and New Zealand Journal of Medicine 9:3, pages 297-301.
Crossref
Samuel Charache. 1978. Oxygen Transport to Tissue — III. Oxygen Transport to Tissue — III 433 441 .

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