Anti-coagulant activity of a metalloprotease: further characterization from the Indian cobra (Naja naja) venom

作者：Kumar M S; Devaraj V R; Vishwanath B S; Kemparaju K^*

来源：Journal of Thrombosis and Thrombolysis, 2010, 29(3): 340-348.

DOI：10.1007/s11239-009-0379-2

• Fibrin(ogen)olytic activity
• SVMPs
• Alpha polymer
• Defibrinogenating activity
• Elapid venom
• Anticoagulant activity

A high molecular mass, non toxic metalloprotease the NN-PF3 with the bound Ca(2+) and Zn(2+) from the Naja naja venom has been studied further for its anticoagulant property. The molecular mass by MALDI-TOF mass spectrometry was 67.81 kDa. The NN-PF3 exhibited fibrin(ogen)olytic activity. In addition to fibrinogen, NN-PF3 hydrolyzed blood and plasma clot with the later hydrolyzed about one fold higher. The alpha polymer of fibrin was preferentially hydrolyzed over the alpha chain but the beta chain and gamma-gamma dimer remained untouched. It was devoid of plasminogen activation property. It prolonged the activated partial thromboplastin time, prothrombin time and the thrombin clotting time of citrated human plasma. It did not affect the thrombin activity. In mice, defibrinogentaion, prolonged bleeding time (P < 0.01) and reduced fibrinogen level were observed following intravenous injection. Human plasma or alpha 2-macroglobulin did not, but the polyvalent anti-venom inhibited the NN-PF3 activity. In contrast to most snake venom metalloproteases, it did not degrade extra cellular matrix proteins.

• 出版日期2010-4