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PURIFICATION OF YEAST CYTOCHROME-C-OXIDASE WITH A SUBUNIT COMPOSITION RESEMBLING THE MAMMALIAN ENZYME

TAANMAN, JW; CAPALDI, RA; (1992) PURIFICATION OF YEAST CYTOCHROME-C-OXIDASE WITH A SUBUNIT COMPOSITION RESEMBLING THE MAMMALIAN ENZYME. J BIOL CHEM , 267 (31) 22481 - 22485. Gold open access

Abstract

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.

Type: Article
Title: PURIFICATION OF YEAST CYTOCHROME-C-OXIDASE WITH A SUBUNIT COMPOSITION RESEMBLING THE MAMMALIAN ENZYME
Open access status: An open access publication
Publisher version: http://www.jbc.org/content/early/recent/0
Keywords: NUCLEAR-CODED SUBUNITS, AMINO-ACID-SEQUENCE, MITOCHONDRIAL-MEMBRANE SYSTEM, GEL-ELECTROPHORESIS, SKELETAL-MUSCLE, DNA-SEQUENCE, BOVINE HEART, PROTEINS, COMPLEX, NITROCELLULOSE
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Clinical and Movement Neurosciences
URI: http://discovery.ucl.ac.uk/id/eprint/51435
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