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黄杆菌对硫磷水解酶及大肠杆菌过氧化氢酶无水解梭曼活性
引用本文:邵 煌 孙曼霁. 黄杆菌对硫磷水解酶及大肠杆菌过氧化氢酶无水解梭曼活性[J]. 中国药理学与毒理学杂志, 1996, 10(2): 157-158
作者姓名:邵 煌 孙曼霁
作者单位:军事医学科学院毒物药物研究所
摘    要:黄杆菌对硫磷水解酶及大肠杆菌过氧化氢酶无水解梭曼活性邵煌孙曼霁(军事医学科学院毒物药物研究所,北京100850)黄杆菌(Flavobacteriumsp.strainATCC27551)和缺陷假单胞菌(PseudomonasdiminutaMG)的对...

关 键 词:梭曼;水解酶类;梭曼水解酶;对硫磷水解酶;过氧化氢酶
收稿时间:1995-07-18

Parathionase of Flavobacterium and catalase of Escherichia coli are incapable of hydrolysing soman
SHAO Huang, SUN Man-Ji. Parathionase of Flavobacterium and catalase of Escherichia coli are incapable of hydrolysing soman[J]. Chinese Journal of Pharmacology and Toxicology, 1996, 10(2): 157-158
Authors:SHAO Huang   SUN Man-Ji
Affiliation:(Institute of Pharmacology & Toxicology, Academy of Military Medical Sciences, Beijing 100850)
Abstract:Somanase locates in the cytosol of Escherichia coli JM105. The transformation of the expression plasmid pWM513 containing parathionase gene of Flavobacterium sp.failed to contribute to the somanase activity of JM105. It suggested that soman was not degradated by parathionase. E. coli UM255, a catalase gene deficient strain, was found to have its endogeneous somanase activity. The transformation of E. coli UM255 with expression plasmid pAMKatE6 bearing the catalase gene of E. coli did not exhibit any influence on somanase level. It implies that somanase activity in E. coli is not the function of catalase and these enzymes are encoded by different genes.
Keywords:soman  hydrolases  somanase  parathionase  catalase
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