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Properties and Primary Structure of the Cytochrome c from the Flight Muscles of the Moth, Samia cynthia

From the ¹ From the Biochemical Research Department, Abbott Laboratories, North Chicago, Illinois 60064

The complete amino acid sequence of the cytochrome c from the flight muscles of a saturnid moth, Samia cynthia, has been established. This protein is functionally and structurally homologous to other mammalian-type cytochromes c. However, it differs from cytochromes c of vertebrate origin by having a nonacetylated NH₂-terminal residue, being 107 rather than 104 residues long and carrying an arginine rather than a lysine at Position 13, immediately before the first thioether-bonded cysteine. These characteristics appear to be common to nonvertebrate cytochromes c, including the bakers' yeast protein. In other primary structure features, S. cynthia cytochrome c resembles the vertebrate more than the yeast proteins, as might be expected from the phylogenetic relations of fungi, invertebrates, and vertebrates.

S. cynthia cytochrome c carries a phenylalanine at Position 65, in place of the methionyl residue found in the other homologous proteins, indicating the lack of a specific requirement for methionine at this position.

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