Abstract
Twenty-seven peptides, including the haemopeptide, were isolated from a single chymotryptic digest of seal heart cytochrome c by chromatography on Sephadex G-75, Whatman phosphocellulose P-70 and Bio-Rad AG 50W-X2. These peptides were purified by electrophoresis or chromatography on paper and their sequences were determined. The complete sequence of the protein was deduced by alignment of these peptides by comparison with the known sequences of several other cytochromes c. Seal cytochrome c differs from the dog and horse proteins in 1 and 6 positions, respectively. The single difference from dog cytochrome c is found in position 100 where isoleucine, in the seal, replaces the lysine found in the dog.
Published Version
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