金黄色葡萄球菌金属蛋白酶对凝血酶原的激活作用。
Prothrombin activation by a metalloprotease from Staphylococcus aureus.
作者信息
Wegrzynowicz Z, Heczko P B, Drapeau G R, Jeljaszewicz J, Pulverer G
出版信息
J Clin Microbiol. 1980 Aug;12(2):138-9. doi: 10.1128/jcm.12.2.138-139.1980.
Abstract
Formation of thrombin during incubation of purified bovine prothrombin with purified staphylococcal metalloprotease has been investigated. Thrombin activity was estimated by examination of clotting time and by digestion of a synthetic substrate, Chromozym TH. The metalloprotease caused direct activation of prothrombin which was inhibited by the addition of ethylenediaminetetraacetic acid. Metalloprotease produced by some strains of Staphylococcus aureus may simulate staphylocoagulase activity.
摘要
对纯化的牛凝血酶原与纯化的葡萄球菌金属蛋白酶孵育过程中凝血酶的形成进行了研究。通过检查凝血时间和消化合成底物Chromozym TH来估计凝血酶活性。金属蛋白酶可直接激活凝血酶原，添加乙二胺四乙酸可抑制这种激活作用。某些金黄色葡萄球菌菌株产生的金属蛋白酶可能模拟葡萄球菌凝固酶活性。
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