Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom

Kasturi, S. and Gowda, T. Veerabasappa (1989) Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom. Toxicon, 27 (2). pp. 229-237. ISSN 0041-0101

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Official URL: http://dx.doi.org/10.1016/0041-0101(89)90136-0

Abstract

S. Kasturi and T. V. Gowda. Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom. Toxicon27, 229–237, 1989.—A major phospholipase A2 (VRV PL-VIIIa) which constitutes 24% of the whole Vipera russelli venom was purified to homogeneity by CM-Sephadex C-25 column chromatography followed by gel filtration on Sephadex G-50. VRV PL-VIIIa is a basic protein with a molecular weight of 11,800 by SDS-PAGE. This enzyme contributes 45% of the total PLA2 activity of the venom, but it is least toxic compared to other purified basic PLA2 enzymes prepared from V. russelli venom. The ld50 value (i.p.) of VRV PL-VIIIa is 5.3 mg/kg body wt. It shows neurotoxic symptoms and damages vital organs such as lung, liver and kidney at ld50 doses. It induces myonecrosis when injected i.m. into the thigh muscle of mice and edema when injected into the foot pads.

Item Type: Article
Additional Information: Unmapped bibliographic data: PY - 1989/// [EPrints field already has value set] JO - Toxicon [Field not mapped to EPrints]
Subjects: Agriculture Biological Sciences > Biochemistry
University of Mysore > PG Campuses > Manasagangotri, Mysore > Agriculture Biological Sciences > Biochemistry
Divisions: PG Campuses > Manasagangotri, Mysore > Biochemistry
Depositing User: Praveen Kumari B.L
Date Deposited: 19 Aug 2013 09:30
Last Modified: 02 Sep 2013 07:51
URI: http://eprints.uni-mysore.ac.in/id/eprint/14801

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