Interaction Between Isolated Cytochrome c1 and Cytochrome c

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Abstract
Cytochrome c1 from bovine heart mitochondria was isolated by a modification of the technique of Koenig et al. (1980) which involved an affinity chromatography step on a gel with yeast [Saccharomyces cerevisiae] 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 MW of 30,000. By using an arylazido derivative of cytochrome c, having the photoactive group bound to lysine 13, a cross-link with the described preparation of cytochrome c1 was obtained upon illumination. By pepsin digestion of the cross-linked complex a limiting fragment was obtained and partially sequenced. It allowed identification of the site of binding of cytochrome c near the sequence 167-174 of cytochrome c1.