Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis

Raghavendra Gowda, C. D. and Nataraju, A. and Rajesh, R. and Dhananjaya, B. L. and Sharath, B. K. and Vishwanath, B. S. (2006) Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis. Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology, 143 (3). 295 - 302.

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Official URL: https://doi.org/10.1016/j.cbpc.2006.03.001


The action of venom proteases and their role in hemostasis has been compared in the venoms of Trimeresurus malabaricus, Daboia russellii and Naja naja from the Southern region of Western Ghats, India. These venoms exhibit varying amounts of proteolytic activity and also influence hemostasis differently. Casein hydrolyzing activity of T. malabaricus venoms was 16 and 24 fold higher than those of N. naja and D. russellii venoms, respectively. With the synthetic substrate TAME, the highest activity was observed in T. malabaricus venom. N. naja venom did not hydrolyze TAME even at higher concentrations. These variations in proteolytic activity also influenced the coagulation process. T. malabaricus and D. russellii venoms are strongly procoagulant and reduce the re-calcification time from 148 to 14 and 12 s, respectively. Similarly, both T. malabaricus and D. russellii venoms reduce the prothrombin time from 12.5 to 6.0 s. On the other hand, N. naja venom is anticoagulant and prolongs re-calcification time to 600 s and prothrombin time to 42 s. In spite of varied effects on hemostasis, all the venoms hydrolyze fibrinogen. T. malabaricus venom hydrolyses both Aα and Bβ subunits. While D. russellii and N. naja venoms hydrolyse only Aα. None of these venoms hydrolyze the γ subunit of fibrinogen. Inhibition studies with specific protease inhibitors revealed that both N. naja and T. malabaricus venoms contain only metalloproteases. D. russellii venom contained both serine and metalloproteases. Only, T. malabaricus venom exhibited thrombin-like activity and induces fibrin clot formation with purified fibrinogen within 58 s. Even though D. russellii venom exhibits procoagulant activity, it did not show thrombin-like activity and may act on other coagulation factors.

Item Type: Article
Uncontrolled Keywords: Coagulant activity, Endemic snake, Fibrinogenase, Thrombin like activity, Hemostasis, Metalloproteases, Western Ghats of India,
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Centre for Geoinformatics Technology
Depositing User: LA manjunath user
Date Deposited: 17 Aug 2019 10:15
Last Modified: 29 Jun 2022 10:08
URI: http://eprints.uni-mysore.ac.in/id/eprint/6683

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