过氧化物酶
化学
谷胱甘肽
谷胱甘肽过氧化物酶
GPX3型
GPX6型
辣根过氧化物酶
GPX1型
GPX4
生物化学
环境化学
谷胱甘肽还原酶
色谱法
酶
作者
Leopold Flohé,W. A. Günzler
出处
期刊:Elsevier eBooks
[Elsevier]
日期:1984-01-01
卷期号:: 114-120
被引量:3881
标识
DOI:10.1016/s0076-6879(84)05015-1
摘要
Publisher Summary To determine glutathione peroxidase reliably, some factors of potential pitfall have to be considered, for example, enzymatic side reactions of substrates (especially when crude tissue samples are assayed), high and variable spontaneous reaction rates of substrates, and the peculiar kinetics of the enzyme itself. With the best documented example, the enzyme of bovine red blood cells, ping-pong kinetics with infinite limiting maximum velocities, and Michaelis constants have been established. This means that the generally recommended conditions for determination of enzyme activity––that is, “saturating” concentrations of all substrates, cannot possibly be fulfilled. In consequence, compromises are inevitable in the choice of substrate concentration for the assay and in the definition of the unit of activity. Fixed-time assay measuring H 2 O 2 consumption and continuous monitoring of Glutathione disulfide (GSSG) formation are cited here. The main differences between the assay procedure described and those proposed by others are listed in the chapter. To compare the results obtained by different procedures, appropriate empirical converting factors are also given.
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