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Oxygen-linked binding sites for inorganic anions to hemoglobin.
A hemoglobin hybrid (alpha 2c beta 2 Prov) in which the alpha chains have NH2-terminal residues that have been blocked specifically by carbamylation and beta chains that have been derived from hemoglobin Providence I (beta 82 Lys leads to Asn) was prepared. This derivative shows a small but significant dependence of its oxygen equilibrium curve on the concentration of chloride, phosphate, or nitrate. These data were compared with oxygen-linked anion binding to hemoglobins A and Providence, and to the carbamylated hybrid, alpha 2c beta 2, by fitting equations to the data with the use of MULTIFIT II, a nonlinear curve-fitting program. Dependence of the anion dissociation constants from deoxygenated (KD) and fully oxygenated (Ko) hemoglobins upon the mathematical model is described. The data provide further support that Val-1 (alpha) and Lys-82 (beta) of hemoglobin are major, oxygen-linked binding sites for small inorganic anions and suggested that a third oxygen-linked site may also be present.
PMID: 7380825 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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From the Arctic to fetal life: physiological importance and structural basis of an 'additional' chloride-binding site in haemoglobin.
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[Biochem J. 2004]
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Properties of a recombinant human hemoglobin with aspartic acid 99(beta), an important intersubunit contact site, substituted by lysine.
Yanase H, Cahill S, Martin de Llano JJ, Manning LR, Schneider K, Chait BT, Vandegriff KD, Winslow RM, Manning JM.
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[Protein Sci. 1994]
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The 'natural' hybrid haemoglobin from mule. Interrelationships with its parent haemoglobins from horse and donkey.
Condò SG, Coletta M, Cicchetti R, Argentin G, Guerrieri P, Marini S, el-Sherbini S, Giardina B.
Biochem J. 1992 Mar 1; 282 ( Pt 2):595-9.
[Biochem J. 1992]