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Microsomal fractions isolated from rat corpus striatum catalyze the oxidation of thiobenzamide to the sulfoxide. The rate of thiobenzamide sulfoxidation is 6.9 +/- 4.8 nmol(min)-1 (mg microsomal protein)-1. The reaction is inhibited by an excess of sulfur- and nitrogen-containing substrates for the microsomal flavin-containing monooxygenase. These inhibitors of thiobenzamide sulfoxidation include methimazole, cysteamine, and trimethylamine. Enzyme activity is also destroyed by treatment of the microsomal preparation at 60 degrees for 1 min. In parallel experiments, rat liver microsomes exhibit similar inhibition characteristics. The data indicate the presence in corpus striatum of a microsomal monooxygenase with catalytic properties of the hepatic microsomal flavin-containing monooxygenase.
M W Duffel, and
S G Gillespie
May 2019,
Xenobiotica; the fate of foreign compounds in biological systems,
M W Duffel, and
S G Gillespie
January 1996,
Methods in enzymology,
M W Duffel, and
S G Gillespie
June 1990,
The Journal of biological chemistry,
M W Duffel, and
S G Gillespie
July 1991,
Biochemical pharmacology,
M W Duffel, and
S G Gillespie
January 1986,
Advances in experimental medicine and biology,
M W Duffel, and
S G Gillespie
January 1987,
Drug metabolism and disposition: the biological fate of chemicals,
M W Duffel, and
S G Gillespie
January 1993,
Life sciences,
M W Duffel, and
S G Gillespie
January 1985,
Drug metabolism and disposition: the biological fate of chemicals,
M W Duffel, and
S G Gillespie
December 1982,
Biochemical and biophysical research communications,
M W Duffel, and
S G Gillespie
January 1981,
Biochemical and biophysical research communications,
