论文部分内容阅读
对E.coli和klebsiella aerogenes提取物中谷胱甘肽合成酶(GS)氧化修饰的详细研究证实这种氧化作用有赖于NAD(P)H、0:和Fe(I)或Cu(I>。对O,和辅助电子供体的需要提示混合功能氧化(MFO)型机制可促进这种氧化作甩。同时也发现MFO系统很容易使多种酶失活,因而使这些酶对某些内源和外源蛋白酶在分解的蛋白质的降解作用有敏感性。也已证实蛋白质的氧化也参与中性粒细胞的细菌杀伤和动物增龄及病理条件下酶类形式(无活性或活性很低)的改变。本文旨在概述MFO系统参与蛋白质氧化作用的机制以及这种氧
A detailed study of the oxidative modification of glutathione synthetase (GS) in E. coli and klebsiella aerogenes extracts confirms that this oxidation depends on NAD (P) H, 0: and Fe (I) or Cu (I> O, and ancillary electron donors suggest that a mixed-function oxidation (MFO) -type mechanism can promote this oxidation. It has also been found that the MFO system can easily inactivate multiple enzymes, thus allowing these enzymes to act on certain endogenous and Exogenous proteases are sensitive to the degradation of the degraded proteins and it has also been demonstrated that protein oxidation is also involved in the bacterial killing of neutrophils and changes in the enzymatic form (low activity or low activity) of animals under aging and pathological conditions This article aims to outline the mechanism by which the MFO system participates in protein oxidation and this oxygen