人肝谷胱甘肽过氧化物酶的动力学性质  

KINETIC PROPERTIES OF HUMANLIVER GLUTATHIONE PEROXIDASE

作　　者：徐蘅[1] 裘奇[1] 胡梅清[1] 

机构地区：[1]南京铁道医学院生物化学教研室

出　　处：《南京铁道医学院学报》1994年第4期198-201,共4页Journal of Nanjing Railway Medical College

摘　　要：从人肝中分离获得谷胱甘肽过氧化物酶，其最适ｐＨ为８．５，最适温度为３７℃。该酶以Ｈ２Ｏ２或ＧＳＨ为底物时表现Ｋｍ值分别为０．２７ｍｍｏｌ／Ｌ和１．３ｍｍｏｌ／Ｌ。酶与多分子底物作用的动力学研究表明人肝谷胱甘肽过氧化物酶的作用为乒乓机制。并观察了一些金属离子和烷化剂对该酶具有不同程度的抑制作用。lutathione peroxidase was purified to homogeneity from human liver;The optimum pH andoptimum temperature of the enzyme were 8.5,37℃,respectively. The apparent Km of the en-zyme for H2O2 was 0.27 mmol/L and for GSH 1.3 mmol/L. Kinetice studies showed that the re-action catlyzed by the enzyme was in accordance with a ping pong mechanism, Some metalionsand alkylating agents were found to be inhibitory to the enzyme activity.

关 键 词：人肝 谷胱甘肽 过氧化物酶 动力学 过氧化反应 

分 类 号：R977.3[医药卫生—药品]