Fowler C J, Oreland L
J Pharm Pharmacol. 1980 Oct;32(10):681-8. doi: 10.1111/j.2042-7158.1980.tb13038.x.
The extraction of lipids from rat liver mitochondrial membranes by 2-butanone treatment inhibited the activity of membrane-bound monoamine oxidase -A but not -B. For the -B form, the apparent Michaelis constants of the enzyme towards oxygen and the maximum molecular turnover numbers obtained when beta-phenethylamine and benzylamine were used as substrates were not significantly changed by the lipid-depletion procedure, but the values of the Michaelis constant towards benzylamine was significantly increased after lipid-depletion. The differential sensitivity of beta-phenethylamine and benzylamine oxidation to inhibition by Tris-HCl was not changed after lipid-depletion. The results are consistent with the hypothesis that the mitochondrial membrane lipids, while essential for the activity of the -A form of the enzyme in rat liver, play a more subtle modulatory role in the activity of the -B form.
用2-丁酮处理从大鼠肝线粒体膜中提取脂质，可抑制膜结合单胺氧化酶-A的活性，但不影响-B的活性。对于-B形式，当使用β-苯乙胺和苄胺作为底物时，该酶对氧的表观米氏常数以及获得的最大分子转换数在脂质耗竭过程后没有显著变化，但脂质耗竭后对苄胺的米氏常数的值显著增加。脂质耗竭后，β-苯乙胺和苄胺氧化对Tris-HCl抑制的差异敏感性没有改变。这些结果与以下假设一致：线粒体膜脂质虽然对大鼠肝脏中该酶的-A形式的活性至关重要，但在-B形式的活性中起更微妙的调节作用。
