Purification and Properties of the Rotenone — Insensitive NADH: Q6 Oxidoreductase from Saccharomyces Cerevisiae

  • Simon de Vries
  • Leslie A. Grivell


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.


NADH Dehydrogenase Single Polypeptide DEAE Column NADH Dehydrogenase Activity Mitochondrial NADH Dehydrogenase 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Simon de Vries
    • 1
  • Leslie A. Grivell
    • 1
  1. 1.Section for Molecular Biology Laboratory of BiochemistryUniversity of AmsterdamAmsterdamThe Netherlands

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