Microsomal flavin-containing monooxygenase activity in rat corpus striatum

J Neurochem. 1984 May;42(5):1350-3. doi: 10.1111/j.1471-4159.1984.tb02794.x.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Corpus Striatum / enzymology*
  • Kinetics
  • Male
  • Microsomes / enzymology*
  • Microsomes, Liver / enzymology
  • Oxidation-Reduction
  • Oxygenases / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Thioamides / metabolism

Substances

  • Thioamides
  • thiobenzamide
  • Oxygenases
  • dimethylaniline monooxygenase (N-oxide forming)