Thromb Haemost 1988; 59(02): 304-309
DOI: 10.1055/s-0038-1642776
Original Articles
Schattauer GmbH Stuttgart

Comparison of the Platelet Aggregation Induced by Three Thrombin-Like Enzymes of Snake Venoms and Thrombin

Che-Ming Teng
The Pharmacological Institute, College of Medicine, National Taiwan University, Taipei, Taiwan
Feng-Nien Ko
The Pharmacological Institute, College of Medicine, National Taiwan University, Taipei, Taiwan
› Author Affiliations
Further Information

Publication History

Received 11 June 1987

Accepted after revision 24 December 1987

Publication Date:
21 May 2018 (online)


Platelet aggregation induced by three thrombin-like enzymes of snake venoms was compared with that by thrombin. Acutin was isolated from Agkistrodon acutus venom and thrombocytin and batroxobin were from Bothrops atrox venom. The fibrinogenclotting activities were 700,170 and 7 U/mg for batroxobin, acutin and thrombocytin, respectively. They induced aggregation and ATP release of washed rabbit platelets. The aggregating activity of thrombin was 102, 104 and 105 times more potent than those of thrombocytin, acutin and batroxobin, respectively. Plateletactivating potency of the thrombin-like enzymes was correlated with their effectiveness on the retractility and elasticity of the clots. Platelet aggregation induced by thrombin or thrombocytin could be inhibited by heparin with antithrombin III while that by acutin or batroxobin could not. Indomethacin showed weak inhibition on the aggregation while the ADP-scavenging system, creatine phosphate/creatine phosphokinase, inhibited the aggregation induced by the three thrombin-like enzymes but not that by thrombin. Platelet aggregation induced by the thrombin-like enzymes could not be inhibited by PAF antagonists-BN 52021, kadsurenone or L-652,731. In the presence of EGTA, only thrombin could induce ATP release from platelets. Thrombin-like enzymes and low concentration of thrombin did not form thromboxane B2. Nitroprusside and prostaglandin E1 completely inhibited the aggregation, mepacrine and imipramine showed marked inhibition while verapamil had only weak inhibition. It is concluded that the aggregation induced by the thrombin-like enzymes is different from that of thrombin and mainly due to ADP released from platelets.