Primary structure of mouse, rat, and guinea pig cytochrome c

Authors:
  • SCSteven S. Carlson
    Steven S. Carlson
  • GMGeorge A. Mross
    George A. Mross
  • AWAllan C. Wilson
    Allan C. Wilson
  • RMRobert T. Mead
    Robert T. Mead
  • LWLawrence D. Wolin
    Lawrence D. Wolin
  • SBSteven F. Bowers
    Steven F. Bowers
  • NFNeal T. Foley
    Neal T. Foley
  • AMA. O. Muijsers
    A. O. Muijsers
  • EME. Margoliash
    E. Margoliash
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Abstract
For immunochemical and evolutionary reasons we determined the primary structure of cytochrome c from two strains of laboratory mice. Thioacetylthioethane and thioacetylthioglycolic acid were used in addition to conventional reagents for sequence determinations. The sequence was found to be identical with that of the rabbit except for residues 44 and 89 and consistent with the peptide compositional data reported by Hennig (Hennig, B. (1975), Eur. J. Biochem. 55, 167-183). The rat cytochrome c cymotryptic peptides were identical with those of the mouse in amino acid composition and amino-terminal residues. Further, peptide maps of cytochromes c of the guinea pig and two strains of rat indicate that all these animals have the same cytochrome c as the laboratory mouse. It is concluded that rodent cytochromes c are evolutionarily conservative and that there is no evidence for a generation-time effect in cytochrome c evolution.