Reference: Taanman JW and Capaldi RA (1992) Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme. J Biol Chem 267(31):22481-5

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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.

Reference Type
Comparative Study | Journal Article | Research Support, U.S. Gov't, P.H.S.
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Taanman JW, Capaldi RA
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