Studies on cytochrome c oxidase, IX. The primary structure of polypeptide VIa.
The complete amino acid sequence of the cytoplasmic polypeptide VIa of cytochrome c oxidase from beef heart is described. The primary structure of this component of complex IV of the respiratory chain is elucidated by isolation and sequencing of overlapping glutamic acid, arginine, tryptophan and methionine fragments obtained by cleavage with Staphylococcus aureus protease, protease from submaxillaris glands of mice, 2-iodosylbenzoic acid and cyanogen bromide. The chain length of polypeptide VIa is 98 amino acids, the resulting molecular mass of 10670 Da. The hydrophilic protein does not contain a hydrophobic membrane penetrating sequence domain. Its function in the respiratory complex IV is unknown.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003488:Cyanogen Bromide; D003576:Electron Transport Complex IV; D009206:Myocardium / Q000201:enzymology; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D013363:Submandibular Gland / Q000201:enzymology
D000596:Amino Acids; D010446:Peptide Fragments; D003576:Electron Transport Complex IV; D010447:Peptide Hydrolases; D003488:Cyanogen Bromide