大鼠心脏中单胺氧化酶和氨基脲敏感胺氧化酶对正戊胺的脱氨基作用。
The deamination of n-pentylamine by monoamine oxidase and a semicarbazide-sensitive amine oxidase of rat heart.
作者信息
Guffroy C, Fowler C J, Strolin Benedetti M
出版信息
J Pharm Pharmacol. 1983 Jul;35(7):416-20. doi: 10.1111/j.2042-7158.1983.tb04314.x.
Abstract
n-Pentylamine is deaminated by homogenates of rat heart. Clorgyline inhibition curves at 10 and 100 microM n-pentylamine indicated that this substrate was deaminated by MAO-A, -B and a clorgyline-resistant amine oxidase sensitive to inhibition by semicarbazide. These results have been compared with two other commonly used monoamine substrates, beta-phenethylamine and benzylamine.
摘要
正戊胺可被大鼠心脏匀浆脱氨基。在10和100微摩尔正戊胺浓度下的氯吉兰抑制曲线表明，该底物可被单胺氧化酶A、B以及一种对氨基脲抑制敏感的耐氯吉兰胺氧化酶脱氨基。这些结果已与另外两种常用的单胺底物β-苯乙胺和苄胺进行了比较。
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