title: Subunit Composition of Cytochrome c Oxidase in Mitochondria of Zea mays.
abstract: Cytochrome c oxidase has been purified from Zea mays mitochondria by a solubilization with dodecyl maltoside followed by a simple and rapid two step fast protein liquid chromatographic method involving anion exchange on Mono Q and size exclusion chromatography on Superose 12. The preparation obtained was resolved by urea sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had a subunit composition comprising polypeptides of apparent molecular masses of 48, 31, and 25 kilodaltons at least one at 16 and 11 kilodaltons and three subunits below 10 kilodaltons. Comparison with a purified yeast cytochrome c oxidase revealed that the four largest subunits showed similar electrophoretic mobilities. Subunits I and II cross-reacted with antibodies raised against the yeast homologous polypeptides. Polypeptides of the plant ubiquinone:cytochrome c reductase complex have also been identified by cross-reaction with antibodies raised against yeast cytochrome b and c(1) subunits and by inference from comigration.
authors: University of Edinburgh, Department of Botany, The Kings Building's, Mayfield Road, Edinburgh, EH9 3JH, Scotland.
authors: M J
authors: MJ
authors: Hawkesford
authors: A D
authors: AD
authors: Liddell
authors: C J
authors: CJ
authors: Leaver