Purification and Properties of the Rotenone — Insensitive NADH: Q6 Oxidoreductase from Saccharomyces Cerevisiae
We report a method for the purification of NADH: Q6 oxidoreductase from mitochondria ofSaccharomyces cerevisiae. The procedure involves the extraction of mitochondria with the non-ionic detergent Triton X-100, followed by DEAE-cellulose chromatography and ‘affinity’ chromatography on Blue-Sepharose. The purified dehydrogenase consists of a single polypeptide, as revealed by Polyacrylamide gel electrophoresis in the presence of SDS, and it contains FAD as prosthetic group. The properties of this enzyme are briefly discussed.
KeywordsNADH Dehydrogenase Single Polypeptide DEAE Column NADH Dehydrogenase Activity Mitochondrial NADH Dehydrogenase
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