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

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...

Parathionase of Flavobacterium and catalase of Escherichia coli are incapable of hydrolysing soman

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.