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Title of Journal: J Thromb Thrombolysis

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Abbravation: Journal of Thrombosis and Thrombolysis

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Springer US

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DOI

10.1007/bf03060095

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1573-742X

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Anticoagulant activity of a metalloprotease furt

Authors: M S Kumar V R Devaraj B S Vishwanath K Kemparaju
Publish Date: 2009/07/23
Volume: 29, Issue: 3, Pages: 340-348
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Abstract

A high molecular mass non toxic metalloprotease the NNPF3 with the bound Ca2+ and Zn2+ from the Naja naja venom has been studied further for its anticoagulant property The molecular mass by MALDITOF mass spectrometry was 6781 kDa The NNPF3 exhibited fibrinogenolytic activity In addition to fibrinogen NNPF3 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  001 and reduced fibrinogen level were observed following intravenous injection Human plasma or α2macroglobulin did not but the polyvalent antivenom inhibited the NNPF3 activity In contrast to most snake venom metalloproteases it did not degrade extra cellular matrix proteins


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