Titration curves of interacting cytochrome b5 and hemoglobin by isoelectric focusing-electrophoresis
Academic Article
Publication Date:
1978
Citation:
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.
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.
IRIS type:
01 - Articolo su periodico
Keywords:
Rats ; L-Lactate Dehydrogenase ; Microsomes, Liver ; Animals ; Cytochromes ; Kinetics ; Hydrogen-Ion Concentration ; Humans ; Nephelometry and Turbidimetry ; Methemoglobin ; Protein Binding ; Isoelectric Focusing
List of contributors:
P.G. Righetti, G. Gacon, E. Gianazza, D. Lostanlen, J.C. Kaplan
Link to information sheet: