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

Kumar, M. S. and Devaraj, V. R. and Vishwanath, B. S. and Kemparaju, K. (2010) Anti-coagulant activity of a metalloprotease: further characterization from the Indian cobra (Naja naja) venom. Journal of Thrombosis and Thrombolysis, 29 (3). pp. 340-348. ISSN 1573-742X

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Abstract

A high molecular mass, non toxic metalloprotease the NN-PF3 with the bound Ca2+ and Zn2+ 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 α polymer of fibrin was preferentially hydrolyzed over the α chain but the β chain and γ—γ 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 α2-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.

Item Type:	Article
Subjects:	C Chemical Science > Biochemistry
Divisions:	Department of > Biochemistry
Depositing User:	LA manjunath user
Date Deposited:	15 Jul 2019 09:57
Last Modified:	15 Jul 2019 09:57
URI:	http://eprints.uni-mysore.ac.in/id/eprint/5199

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