Abstract
While the hepatotoxicant thiobenzamide is S-oxidized primarily by the microsomal FAD-containing monooxygenase, a significant part of the oxidation in mouse liver is due to the cytochrome P-450-dependent monooxygenase system. The oxidation of thiobenzamide by both the FAD-containing monooxygenase and the cytochrome P-450 monooxygenase system was demonstrated using purified enzymes from mouse liver. An inhibitor of the cytochrome P-450 monooxygenase system reduced the overall oxidation of thiobenzamide by approximately 30 percent in microsomes from uninduced mouse liver. One form of cytochrome P-450 purified from rabbit lung was also active in the oxidation of thiobenzamide.
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