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通过钙刺激的磷脂酶A2对透化线粒体中琥珀酸脱氢酶激活的研究。

Study of the succinate dehydrogenase activation in permeabilized mitochondria through the Ca(2+)-stimulated phospholipase A2.

作者信息

Levrat C, Louisot P

机构信息

Department of Biochemistry INSERM-CNRS U189, Oullins, France.

出版信息

Biochem Mol Biol Int. 1994 Oct;34(3):569-78.

PMID:7833834
Abstract

The development of a mitochondrial membrane permeability triggered by the Ca(2+)-stimulation of PLA2 (phospholipase A2; EC 3.1.1.4.) and based on swelling, polyunsaturated fatty acids release and calcium influx, induced the activation of SDH (succinate dehydrogenase; EC 1.3.9.9.) without damaging mitochondria structures. The activity of SDH increased within the length of permeabilization treatment before reaching a plateau. The study of Km and Vm showed that the affinity of SDH for succinate and the maximal velocity were increased. Based on these results, the change of SDH activity triggered under these conditions could be explained by a substrate activation of SDH taking account that the succinate content was significantly enhanced.

摘要

由磷脂酶A2(PLA2;EC 3.1.1.4)的Ca(2+)刺激引发的线粒体膜通透性变化,基于肿胀、多不饱和脂肪酸释放和钙内流,在不破坏线粒体结构的情况下诱导了琥珀酸脱氢酶(SDH;EC 1.3.9.9)的激活。在达到平台期之前,SDH的活性在通透化处理期间增加。对Km和Vm的研究表明,SDH对琥珀酸的亲和力和最大速度都增加了。基于这些结果,考虑到琥珀酸含量显著增加,在这些条件下引发的SDH活性变化可以用SDH的底物激活来解释。

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