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3. Vanadium: genetical and biochemical investigations.

Author

Bronzetti G, Morichetti E, Della Croce C, Del Carratore R, Giromini L, and Galli A

Subjects
7-Alkoxycoumarin O-Dealkylase metabolism, Aminopyrine N-Demethylase metabolism, Animals, Cytochrome P-450 Enzyme System metabolism, Mice, Oxidoreductases, O-Demethylating metabolism, Submitochondrial Particles enzymology, Mutation, Saccharomyces cerevisiae drug effects, Submitochondrial Particles drug effects, Vanadium toxicity
Abstract

Ammonium metavanadate was studied for its ability to induce mitotic gene conversion and reverse point mutation in the D7 strain of Saccharomyces cerevisiae. Metavanadate increased the convertant and revertant frequencies; the highest activity was observed without metabolic activation. This indicated that the S9 hepatic fraction and yeast cells in logarithmic phase (and containing a high level of cytochrome P450) biotransform vanadate, probably reducing it to vanadyl. In addition, the effect of ammonium metavanadate on the hepatic monooxygenase system was studied in mice by measuring the level of cytochrome P450 and determining the activities of aminopyrine N-demethylase, p-nitroanisole O-demethylase and 7-ethoxycoumarin O-deethylase in mouse liver microsomal fraction. The results indicated that this compound reduced mono-oxygenase activity and also the level of cytochrome P450.

Published
1990
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