Duffel M W, Gillespie S G
J Neurochem. 1984 May;42(5):1350-3. doi: 10.1111/j.1471-4159.1984.tb02794.x.
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.
从大鼠纹状体分离出的微粒体部分可催化硫代苯甲酰胺氧化为亚砜。硫代苯甲酰胺亚砜化的速率为6.9±4.8 nmol（分钟）-1（毫克微粒体蛋白）-1。该反应受到微粒体含黄素单加氧酶的过量含硫和含氮底物的抑制。这些硫代苯甲酰胺亚砜化的抑制剂包括甲巯咪唑、半胱胺和三甲胺。通过在60℃下处理微粒体制剂1分钟，酶活性也会被破坏。在平行实验中，大鼠肝脏微粒体表现出相似的抑制特性。数据表明纹状体中存在一种具有肝微粒体含黄素单加氧酶催化特性的微粒体单加氧酶。
