A strong interaction between cytochrome b5 and hemoglobin has been demonstrated by titration curves in isoelectric focusing - electrophoresis. The pH of maximum interaction is in the pH range 8.0-8.3, which suggests a predominant role of Lys of met hemoglobin in the binding to acidic amino acids of cytochrome b5. The stoichiometry of the complex appears to be 1:1 (cytochrome b5: hemoglobin subunit) with similar binding affinities for α and β chains.
Titration curves of interacting cytochrome b5 and hemoglobin by isoelectric focusing-electrophoresis / P.G. Righetti, G. Gacon, E. Gianazza, D. Lostanlen, J.C. Kaplan. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 85:4(1978 Dec 29), pp. 1575-1581.
Titration curves of interacting cytochrome b5 and hemoglobin by isoelectric focusing-electrophoresis
E. Gianazza;
1978
Abstract
A strong interaction between cytochrome b5 and hemoglobin has been demonstrated by titration curves in isoelectric focusing - electrophoresis. The pH of maximum interaction is in the pH range 8.0-8.3, which suggests a predominant role of Lys of met hemoglobin in the binding to acidic amino acids of cytochrome b5. The stoichiometry of the complex appears to be 1:1 (cytochrome b5: hemoglobin subunit) with similar binding affinities for α and β chains.
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