Abstract
Starting with a basic ancestral structure natural selection has provided various ways by which different living species have adapted hemoglobin functions to their respiratory requirements, oxygen transport and the buffering of protons released in the reaction of carbon dioxide with water.
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References
Arnone A (1972) X-ray diffraction study of binding of 2,3 diphosphoglycerate to human haemoglobin. Nature (London) 237: 146–149
Arnone A, Williams DJ (1977) Crystallographic evidence for anion binding sites at the NH2-termini of OL subunits of human deoxy hemoglobin. In Molecular Interactions of Haemoglobin, INSERM Paris, pp. 15–22
Benesch RE, Benesch R (1974) The mechanism of interaction of red cell organic phosphates with hemoglobin. Adv. Protein Chem. 28: 211–237
Bonaventura J, Bonaventura C, Sullivan B, Ferruzzi G, Mc Curdy PR, Fox J, Moo-Penn WF (1978) Hemoglobin Providence. Functional consequences of two alterations of the 2,3 diphosphoglycerate binding site at position ß 82. J. Biol. Chem. 251: 7563–7571
Bonaventura C, Bonaventura J (1978) Anionic control of hemoglobin function. In: Caughey WS (ed) Biochemical and Clinical Aspects of Hemoglobin Abnormalities. Academic Press, New York, pp. 647–661
Bunn HF, Forget BG, Ranney HM (1977) Human Hemoglobins. Saunders, WB, Philadelphia
Fermi, G, Perutz MF (1981) In: Philipps DC and Richards FM (eds) Atlas of Molecular Structures in Biology. 2. Haemoglobin and Myoglobin. Clarendon Press, Oxford, UK
Harano K, Harano T, Shibata S, Ueda S, Mori H, Seki M (1984) Hb Okasaki (ß 93 (F9 Cys→Arg) a new hemoglobin variant with increased oxygen affinity and instability. FEBS Lett. 173: 45–47
International Hemoglobin Information Center (IHIC) (1984) Hemoglobin, 8: 243–300
Kilmartin JV, Wootton JF (1970) Inhibition of Bohr effect after removal of C-terminal histidines from haemoglobin ß-chains. Nature (London) 228: 766–767
Kilmartin JV, Arnone A, Fogg J (1977) Specific modification of the a-chain C-terminal carboxyl group of hemoglobin by trypsin catalyzed hydrazinolysis. Biochemistry 16: 5393–5397
Kilmartin JV, Imai K, Jones RT, Faruqui AR, Fogg J, Baldwin JM (1978) Role of Bohr group salt bridges in cooperativity in hemoglobin. Biochim. Biophys. Acta 534: 15–25
Kilmartin JV, Fogg JH, Perutz MF (1980) Role of the C-terminal histidine in the alkaline Bohr effect of human hemoglobin. Biochemistry 19: 3189–3193
Manning JM, Nigen AM (1978) Major sites for the oxygen-linked binding of chloride to hemoglobin. In: Caughey WS (ed) Biochemical and Clinical Aspects of hemoglobin Abnormalities. Academic Press, New York, pp. 687–694
O’Donnell S, Mandaro R, Shuster T, Arnone A (1979) X-ray diffraction and solution studies of specifically carbamylated human hemoglobin Amer. J. Biol. Chem. 254: 12204–12208
Pettigrew DW, Romeo PH, Tsapis A, Thillet J, Smith ML, Turner BW, Ackers GK (1982) Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin. Proc. Natl. Acad. Sci. USA 79: 1849–1853
Perutz MF, Lehmann H (1968) Molecular pathology of human haemoglobin. Nature 219: 902–909
Perutz MF (1970) Stereochemistry of cooperative effects in haemoglobin. Nature (London) 228: 726–739
Perutz MF, Imai K (1980) Regulation of oxygen affinity of mammalian haemoglobins. J. Mol. Biol. 136: 183–191
Perutz MF, Kilmartin JV, Nishikura K, Fogg JH, Butler PJG, Rollema HS (1980) Identification of residues contributing to the Bohr effect of human haemoglobin. J. Mol. Biol. 138: 649–670
Perutz MF, Brunori M (1982) Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature (London) 299: 421–426
Perutz MF (1983) Species adaptation in a protein molecule. Mol. Biol. Evol. 1: 1–28
Poyart C, Bursaux E, Arnone A, Bonaventura J, Bonaventura C (1980) Structural and functional studies of hemoglobin Suresnes. J. Biol. Chem. 255: 9465–9473
Rochette J, Righetti PG, Bianchi Bosisio A, Vertongen A, Schnek G, Wacjman H (1984) Immobilized pH gradients and reversed-phase high performance liquid chromatography: a strategy for characterization of haemoglobin variants with electrophoretic mobility identical to that of HbA. J. Chromatogr. 285: 143–152
Rochette J, Varet B, Boissel JP, Clough K, Labie D, Wacjman H, Bohn B, Magne Ph, Poyart C (1984) Structure and function of Hb St-Jacques (α2 ß2 140 (H18) Ala→Thr): a new high oxygen-affinity variant with altered bisphosphoglycerate binding. Biochim. Biophys. Acta, 785: 14–21
Rosa R, Prehu MO, Beuzard Y, Rosa J (1978) The first case of a complete deficiency of diphosphoglycerate mutase in human erythrocytes. J. Clin. Invest. 62: 907–915
Wiechelman KJ, Fox J, Mc Curdy PR, Ho C (1978) Proton nuclear resonance studies of Hemoglobin Providence. Biochemistry 17: 791–79
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Poyart, C., Bursaux, E., Galacteros, F., Wacjman, H. (1985). Abnormal Human Hemoglobins: Molecular Tools to Study Normal Hemoglobin Functions. In: Lamy, J., Truchot, JP., Gilles, R. (eds) Respiratory Pigments in Animals. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70616-5_11
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DOI: https://doi.org/10.1007/978-3-642-70616-5_11
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