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猪肝线粒体中单胺氧化酶的底物特异性。

Substrate specificity of monoamine oxidase in pig liver mitochondria.

作者信息

Ekstedt B

出版信息

Med Biol. 1979 Aug;57(4):220-3.

PMID:513878
Abstract

In pig liver both the A and the B form of monoamine oxidase (MAO) were found to be responsible for the oxidation of 5-hydroxytryptamine (5HT), a substrate oxidised by the A form alone in most other tissues. With increasing concentrations of this substrate, the percentage of the substrate oxidised by the B form increased. The Km value of the A and the B form of MAO for 5HT was 200 microns and 2.2 mM, respectively. It is suggested that the division of the monoamines into A and B form substrates should be done on the basis of the molecular turnover numbers rather than on their activities, and that the substrate specificities of the two forms of MAO should be determined over a large range of substrate concentrations.

摘要

在猪肝中发现,单胺氧化酶(MAO)的A和B两种形式都可氧化5-羟色胺(5HT),而在大多数其他组织中,5HT这种底物仅由A形式氧化。随着该底物浓度的增加,由B形式氧化的底物百分比增加。MAO的A和B两种形式对5HT的米氏常数(Km值)分别为200微摩尔和2.2毫摩尔。有人提出,单胺应根据分子周转数而非活性分为A和B两种形式的底物,并且两种形式的MAO的底物特异性应在较大范围的底物浓度下确定。

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