The amino acid sequence of cytochrome c from Helix aspersa Müller (garden snail).
The amino acid sequence of a snail cytochrome c has been determined. The molecule consists of a single polypeptide chain of 104 residues, and is homologous with other mitochondrial cytochromes c. Unlike the cytochromes c from vertebrates, there is no acetyl blocking group at the N-terminus. A change in an otherwise invariant position has been observed in position 87. Comparison with amino acid sequences of cytochromes c from other sources indicates that the point of divergence of the molluscs and the vertebrates in evolutionary time was 720 million years ago. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50009 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972), 126, 5.
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D003574:Cytochrome c Group / Q000032:analysis*; D008928:Mitochondria; D010455:Peptides / Q000032:analysis; D012908:Snails
D003574:Cytochrome c Group; D010455:Peptides