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Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme.
Institute of Molecular Biology, University of Oregon, Eugene 97403.
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.
PMID: 1331058 [PubMed - indexed for MEDLINE]
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Cited by 7 PubMed Central articles
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Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast.
Horan S, Bourges I, Taanman JW, Meunier B.
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ReviewThe mitochondrial oxidative phosphorylation proteome of Chlamydomonas reinhardtii deduced from the Genome Sequencing Project.
Cardol P, González-Halphen D, Reyes-Prieto A, Baurain D, Matagne RF, Remacle C.
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[Plant Physiol. 2005]
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The ORD1 gene encodes a transcription factor involved in oxygen regulation and is identical to IXR1, a gene that confers cisplatin sensitivity to Saccharomyces cerevisiae.
Lambert JR, Bilanchone VW, Cumsky MG.
Proc Natl Acad Sci U S A. 1994 Jul 19; 91(15):7345-9.
[Proc Natl Acad Sci U S A. 1994]
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