Abstract
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.
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