The subunit structure of the cytochrome c oxidase complex.
The subunit structure of the cytochrome c oxidase complex has been obtained for three preparations each isolated by a different detergent procedure. Six polypeptides were present in all samples with the following molecular weights: subunits I, 36000; II, 22500, III, 17100; IV, 12500; V, 9700; and VI, 5300. These subunits have been purified by gel filtration in sodium dodecyl sulfate or in 6 M guanidine hydrochloride and their amino acid compositions have been determined. Subunit I is hydrophobic in character with a polarity of 35.7%. Subunits II through VI are more hydrophilic with polarities of 45.5, 48.6, 47.8, 49.7, and 53.7%, respectively.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003574:Cytochrome c Group; D003902:Detergents; D003576:Electron Transport Complex IV / Q000032:analysis / Q000302:isolation & purification; D046911:Macromolecular Substances; D008931:Mitochondria, Muscle / Q000201:enzymology; D008970:Molecular Weight; D009206:Myocardium
D000596:Amino Acids; D003574:Cytochrome c Group; D003902:Detergents; D046911:Macromolecular Substances; D003576:Electron Transport Complex IV