title: Purification of all thirteen polypeptides of bovine heart cytochrome c oxidase from one aliquot of enzyme. Characterization of bovine fetal heart cytochrome c oxidase.
abstract: A protocol has been worked out for separating all thirteen different polypeptides in the beef heart cytochrome c oxidase complex from a single aliquot of enzyme. This involves an initial separation of polypeptides by gel filtration on a Biogel P-60 column in SDS, a step which purifies subunits CIV and CVIII and gives mixtures of CV + CVI, ASA, AED and STA, as well as CVII, CIX and IHQ. These mixtures are then resolved by reverse-phase high-performance liquid chromatography. The separation procedures have been applied to fetal heart cytochrome c oxidase of gestation between 100 and 200 days. No differences were found in the N-terminal sequences of any of the cytoplasmically made subunits or in the entire sequence of CIX between late fetal and adult forms of the enzyme.
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D006321:Heart / Q000196:embryology; D009206:Myocardium / Q000201:enzymology*
chemical_list: D003576:Electron Transport Complex IV