미토콘드리아와 Cytochrome c 결합에 미치는 염기성 화합물의 영향

• Published in: BMB reports Vol. 20; no. 2; pp. 108 - 116
• Main Authors: 박광숙, Suhas Desi, 박인국, 전길자, 김상덕, 백운기, Kwang Sook Park, In Kook Park, Gil Ja Jun, Sang Duk Kim, Woon Ki Paik
• Format: Journal Article
• Language: Korean
• Published: 생화학분자생물학회 01.01.1987
• ISSN: 1976-6696

Binding of horse heart (methyl-^(14)C)cytochrome c reductively methylated with (^(14)C) formaldehyde to isolated rat liver mitochondria has been investigated. The number of binding sites is calculated to be 56 pmoles of cytochrome c/㎎ of mitochondria) protein, and the affinity constant (K_a) to be 1.79 × 107M^(-1). Various naturally occurring basic compounds including histones, protamine and polyamines are highly inhibitory on the (methyl-^(14)C)cytochrome c binding. Almost all of (methyl-^(14)C)cytochrome c bound to mitochondria can be released from the mitochondria by subsequent treatment with nonlabeled cytochrome c. Although histone H3 (arginine-rich histone) has much stronger inhibitory effect on the (methyl-^(14)C)cytochrome c binding than non-labeled cytochrome c at equimolar concentration when present in the binding assay mixture, only a fraction of bound (methyl-^(14)C)cytochrome c can be freed from mitochondria by treatment with histone H3. Evidence indicates that these effect are not merely a consequence of electrostatic influence on the cytochorme c receptor of mitochondria.