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[大鼠脑单胺氧化酶催化特性变化的可能机制]

[Possible mechanism of the change in the catalytic properties of brain monoamine oxidase in rats].

作者信息

Goroshinskaia I A

出版信息

Biull Eksp Biol Med. 1985 Jun;99(6):672-4.

PMID:4016257
Abstract

An over two-fold decrease in the affinity of mitochondrial MAO to serotonin was found under hyperoxia, hypoxia and cold stress. At the same time serotonin deaminase and glucosamine deaminase activity was detected in the supernatant obtained after precipitation of the mitochondria. The data obtained indicate that the modification of the catalytic properties of MAO is caused both by alteration of the molecular properties of the enzyme and structural derangement of the mitochondrial membranes.

摘要

在高氧、缺氧和冷应激条件下,发现线粒体单胺氧化酶(MAO)对血清素的亲和力下降了两倍多。与此同时,在线粒体沉淀后获得的上清液中检测到血清素脱氨酶和葡糖胺脱氨酶活性。所获得的数据表明,MAO催化特性的改变是由酶分子特性的改变和线粒体膜的结构紊乱共同引起的。

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