Squalene Epoxidase of Rat Liver*

نویسنده

  • James Bryant
چکیده

The microsomal enzyme system from rat liver which catalyzes the epoxidation of squalene to 2,3-oxidosqualene (squalene epoxidase) has been investigated further with 10 ,ll-dihydrosqualene as the artacial substrate. Liver supernatant contributes two essential components to the epoxidase system, one heat stable and the other heat labile (YAMAMOTO, S., AND BLOCH, K. (1970) J. Biol. Chem. 245, 1670). The requirement for the heat-stable factor can be fully met by phosphatidylserine, phosphatidylglycerol, or phos phatidylinositol and partially by other phospholipids. The heat-labile supernatant component is a protein, molecular weight 44,000, which has been purified 84-fold. Supernatant protein factor fails to bind either squalene, 10 ,llDihydrosqualene, or 2,3-oxidosqualene as judged by chromatography of mixtures on Sephadex. In an epoxidase system reconstituted from washed microsomes, supernatant protein factor, and phosphatidylserine, FAD raises enzyme activity by about 50%.

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Studies on Squalene Epoxidase of Rat Liver*

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تاریخ انتشار 2002