title: Studies on cytochrome-c oxidase, XIII. Amino-acid sequence of the small membrane polypeptide VIIIc from bovine heart respiratory complex IV.
abstract: The isolation and complete amino-acid sequence analysis of the cytoplasmically synthesized polypeptide VIIIc from bovine heart cytochrome-c oxidase is described. The protein is a stoichiometric constituent of the mitochondrial respiratory complex IV. Its primary structure is deduced from N-terminal sequencing and peptides obtained by enzymatic cleavage with Staphylococcus aureus proteinase and chemical cleavage with cyanogen bromide. The small protein consists of 56 amino acids summing up to a total Mr of 6243. From position 34 to 51 the chain contains a hydrophobic sequence of 18 residues. This probably membrane-spanning segment also contains the 2 cysteine residues of the chain. The function of this subunit in the respiratory complex IV is still unknown.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D003488:Cyanogen Bromide; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013045:Species Specificity
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D010455:Peptides; D003576:Electron Transport Complex IV; D003488:Cyanogen Bromide