从海栖热袍菌中纯化和性质研究一种高活性的有机磷酸酐酶。
Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina.
机构信息
U.S. Army Chemical and Biological Defense Agency, Edgewood Research, Development and Engineering Center, Research and Technology Directorate, Aberdeen Proving Ground, Maryland 21010-5423.
出版信息
Appl Environ Microbiol. 1993 Sep;59(9):3138-40. doi: 10.1128/aem.59.9.3138-3140.1993.
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.
从海栖热袍菌（Alteromonas undina）中纯化得到一种高活性的有机磷酸酐酶，该酶纯品为单一条肽链，分子量为 53000。以二异丙基氟磷酸（diisopropylfluorophosphate）为底物，该酶的比活约为 575 mumol/min/mg 蛋白。该酶最适 pH 值和温度分别为 8.0 和 55°C，受巯基还原剂和锰离子的激活。它能够快速水解多种神经毒剂和几种显色膦酸酯类化合物。
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