Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme.
Yeast cytochrome c oxidase has been isolated by ion exchange chromatography using lauryl maltoside (n-dodecyl beta-D-maltoside) as the solubilizing detergent. The enzyme prepared in this way has a heme aa3 concentration of 8-9 nmol/mg of protein and a turnover number in the range of 180-210 s-1 at pH 6.2 in 0.01% lauryl maltoside at 20 degrees C. Yeast cytochrome c oxidase prepared by any of several previously published methods which use Triton X-100 contains nine subunits. The enzyme isolated in lauryl maltoside contains these same nine different polypeptides and three others, including homologues of subunits VIa and VIb of the mammalian enzyme.
Taanman
J W
JW
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Capaldi
R A
RA
D000595:Amino Acid Sequence; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000302:isolation & purification*; D007425:Intracellular Membranes / Q000201:enzymology; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D016415:Sequence Alignment; D013057:Spectrum Analysis
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003576:Electron Transport Complex IV