Abstract
Vitamin K epoxide reductase and vitamin K-dependent carboxylase have been solubilized by treatment of rat liver microsomes with potassium cholate. Both reactions required dithiothreitol, and were inhibited by warfarin. NADH did not replace the dithiothreitol requirement. Cytosol stimulated the rate of reduction of vitamin K epoxide four to five fold but was inactive alone. The carboxylation reaction proceeded equally well with vitamin K or vitamin K epoxide. The enzyme activities are stable when stored at −70°. Vitamin K epoxidase activity could not be detected.
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