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来自大肠杆菌的PAPS还原酶:作为硫氧还蛋白探针的酶的特性

PAPS-reductase from Escherichia coli: characterization of the enzyme as probe for thioredoxins.

作者信息

Schwenn J D, Schriek U

出版信息

Z Naturforsch C J Biosci. 1987 Jan-Feb;42(1-2):93-102. doi: 10.1515/znc-1987-1-216.

Abstract

PAPS-reductase from Escherichia coli was employed to detect thioredoxins from pro- and eukaryotic organisms. A simple method for the isolation of this enzyme and properties of the enzymatic assay were described. A comparison between thioredoxins detected by the PAPS-reductase and the Fructose-bisphosphatase or NADP malate dehydrogenase was used to assess the validity of the test. The high cross-reactivity of the bacterial enzyme was useful in the purification of heterologous thioredoxins from spinach, Synechococcus, and Saccharomyces cerevisiae.

摘要

利用来自大肠杆菌的PAPS还原酶检测原核生物和真核生物中的硫氧还蛋白。描述了一种分离该酶的简单方法及酶促测定的性质。通过比较PAPS还原酶检测到的硫氧还蛋白与果糖二磷酸酶或NADP苹果酸脱氢酶,来评估该测试的有效性。这种细菌酶的高交叉反应性有助于从菠菜、聚球藻和酿酒酵母中纯化异源硫氧还蛋白。

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