Studies on cytochrome c oxidase, II. The chemical constitution of a short polypeptide from the beef heart enzyme.
A low molecular weight (approximately 6000) polypeptide fraction was isolated from beef heart cytochrome c oxidase, consisting of three peptides with the N-terminal end groups isoleucine, phenylalanine and serine. The complete amino acid sequence of the serine component is described. From the chemical constitution, a site-specific cleavage from a precursor protein and a possible function in membrane penetration and complex formation of the oxidase is inferred.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003574:Cytochrome c Group; D003576:Electron Transport Complex IV / Q000032:analysis*; D066298:In Vitro Techniques; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification*; D011487:Protein Conformation
D000596:Amino Acids; D003574:Cytochrome c Group; D010446:Peptide Fragments; D003576:Electron Transport Complex IV