Abstract
The alcohol dehydrogenase of microsomal oxidative sterol demethylation is removed from rat liver microsomes by extraction with Tris-acetate buffer. Demethylase activity is reconstituted by addition of either the crude extract or crystalline alcohol dehydrogenase to washed microsomes. The overall reaction catalyzed by the reconstituted system is the same stoichiometrically as that catalyzed by unwashed microsomes. The dehydrogenase of sterol demethylation that catalyzes the oxidation of the primary alcohol may be identical to liver alcohol dehydrogenase.
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Schedule a callMore From: Biochemical and biophysical research communications
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