Interaction between isolated cytochrome c1 and cytochrome c.
Cytochrome c1 from bovine heart mitochondria was isolated by a modification of the technique of König et al. [(1980) Biochim. Biophys. Acta 621, 283-295] which involved an affinity chromatography step on a gel with yeast cytochrome c as a ligand. Its spectra, electrophoretic pattern in presence of sodium dodecylsulfate, its reducibility by ascorbate and cytochrome c were characteristic of a native cytochrome, with a single polypeptide having an apparent molecular weight of 30 000. By using an arylazido derivative of cytochrome c, having the photoactive group bound to lysine 13, upon illumination a cross-link with the described preparation of cytochrome c1 was obtained. By pepsin digestion of the cross-linked complex a limiting fragment was obtained and partially sequenced. It allowed to identify the site of binding of cytochrome c near the sequence 167-174 of cytochrome c1.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003432:Cross-Linking Reagents; D003574:Cytochrome c Group / Q000031:analogs & derivatives; D003575:Cytochromes c1; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses
D003432:Cross-Linking Reagents; D003574:Cytochrome c Group; D003575:Cytochromes c1