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多头绒泡菌苹果酸脱氢酶:线粒体和上清液同工酶的抑制剂分析

Physarum polycephalum malate dehydrogenase: inhibitor analyses of the mitochondrial and supernatant isozymes.

作者信息

Teague W M, Henney H R

出版信息

Can J Microbiol. 1977 May;23(5):589-95. doi: 10.1139/m77-085.

DOI:10.1139/m77-085
PMID:559534
Abstract

The effects of naturally occurring metabolites were tested on the malate dehydrogenase (L-malate: NAD+oxidoreductase, EC 1.1.1.37) isozymes from the eucaryotic protist Physarum polycephalum. Several of the Krebs cycle intermediates were inhibitors for each isozyme indicating that a similar catalytic process was involved for both forms. The metabolites ATP, ADP, and AMP were inhibitors competitive with NAD for the mitochondrial isozyme but not the supernatant form. Several other nucleoside phosphates had no effects. Tests of protein sulfhydryl, arginine- and tyrosine-modifying reagents revealed a similar functional sensitivity by both isozymes to these reagents. Those results are compared with data on isozymes from more complex tissue with comments on the physiological significance of those combined data.

摘要

测试了天然存在的代谢产物对真核原生质体多头绒泡菌中苹果酸脱氢酶(L-苹果酸:NAD⁺氧化还原酶,EC 1.1.1.37)同工酶的影响。几种三羧酸循环中间体对每种同工酶均有抑制作用,这表明两种形式都涉及类似的催化过程。代谢产物ATP、ADP和AMP是线粒体同工酶与NAD竞争的抑制剂,但对上清液形式的同工酶无此作用。其他几种核苷磷酸则无影响。对蛋白质巯基、精氨酸和酪氨酸修饰试剂的测试表明,两种同工酶对这些试剂具有相似的功能敏感性。将这些结果与来自更复杂组织的同工酶数据进行了比较,并对这些综合数据的生理意义进行了评论。

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Physarum polycephalum malate dehydrogenase: inhibitor analyses of the mitochondrial and supernatant isozymes.多头绒泡菌苹果酸脱氢酶:线粒体和上清液同工酶的抑制剂分析
Can J Microbiol. 1977 May;23(5):589-95. doi: 10.1139/m77-085.
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