Guan L F, Chi C W, Yuan M
Thromb Res. 1984 Aug 1;35(3):301-10. doi: 10.1016/0049-3848(84)90361-x.
Three components with arginine esterase activities were found in the venom of the Chinese pit viper (Agkistrodon halys Pallas). They were identified as bradykinin releasing, thrombin-like and fibrinogenolytic enzymes respectively. The thrombin-like enzyme of A. halys Pallas was purified to a homogeneous state. It was a glycoprotein with molecular weight of about 43,000. Though this enzyme displayed a higher esterase activity on BAEE than trypsin and human thrombin, it showed very weak clotting ability on fibrinogen. The kinetic analysis of the release of fibrinopeptides A (FPA) and B (FPB) showed that the action mode of this enzyme on fibrinogen was just opposite to that of mammalian thrombin. FPB was first released, followed by FPA after a long lag period.
在中国蝮蛇（Agkistrodon halys Pallas）的毒液中发现了三种具有精氨酸酯酶活性的成分。它们分别被鉴定为缓激肽释放酶、类凝血酶和纤维蛋白溶解酶。将蝮蛇（Agkistrodon halys Pallas）的类凝血酶纯化至均一状态。它是一种分子量约为43,000的糖蛋白。尽管该酶对苯甲酰-L-精氨酸乙酯（BAEE）的酯酶活性高于胰蛋白酶和人凝血酶，但它对纤维蛋白原的凝血能力非常弱。纤维蛋白肽A（FPA）和B（FPB）释放的动力学分析表明，该酶对纤维蛋白原的作用模式与哺乳动物凝血酶的作用模式正好相反。首先释放FPB，经过较长的延迟期后再释放FPA。
