Open AccessSubunit Composition of Cytochrome c Oxidase in Mitochondria of Zea mays
Author(s) -
Malcolm J. Hawkesford,
A. Liddell,
Christopher J. Leaver
Publication year - 1989
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.91.4.1535
Subject(s) - cytochrome c oxidase , sodium dodecyl sulfate , protein subunit , biochemistry , cytochrome , gel electrophoresis , chemistry , oxidase test , yeast , coenzyme q – cytochrome c reductase , polyacrylamide gel electrophoresis , size exclusion chromatography , cytochrome b , cytochrome c1 , chromatography , cytochrome c , mitochondrion , biology , enzyme , mitochondrial dna , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom