PURIFICATION AND PROPERTIES OF A HIGHLY-ACTIVE ORGANOPHOSPHORUS ACID ANHYDROLASE FROM ALTEROMONAS-UNDINA

被引：86

作者：

CHENG, TC

HARVEY, SP

STROUP, AN

机构：

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 1993年 / 59卷 / 09期

关键词：

D O I：

10.1128/AEM.59.9.3138-3140.1993

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A highly active organophosphorus acid anhydrolase from Alteromonas undina was purified to homogeneity and found to be composed of a single polypeptide chain with a molecular weight of 53,000. With diisopropylfluorophosphate as a substrate, the purified enzyme has a specific activity of approximately 575 mumol/min/mg of protein. The enzyme has optimum activity at pH 8.0 and 55-degrees-C and is stimulated by sulfhydryl reducing agents and manganese. It is capable of rapidly hydrolyzing a wide range of nerve agents and several chromogenic phosphinates.

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页码：3138 / 3140

页数：3

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