Dissociation of enzymatic activity from toxic properties of the most basic phospholipase A2 from Vipera russelli snake venom by guanidination of lysine residues

Babu, A. S. and Veerabasappa Gowda, T. (1994) Dissociation of enzymatic activity from toxic properties of the most basic phospholipase A2 from Vipera russelli snake venom by guanidination of lysine residues. Toxicon, 32 (6). pp. 749-752.

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Official URL: https://doi.org/10.1016/0041-0101(94)90344-1

Abstract

The most basic phospholipase A(2) VRV-PL-VIIIa purified from Russell's viper venom is a toxic enzyme. It induced neurotoxicity, myotoxicity, and oedema and was lethal to mice at 5.3 mu g/g body weight. It also inhibited the coagulation of the human plasma. The epsilon-amino groups of lysine residues of the toxic enzyme VRV-PL-VIIIa were guanidinated with o-methylisourea. Guanidination of the enzyme did not alter the enzymatic activity markedly. The guanidinated enzyme became non-lethal in doses up to 16 mu g/g body weight, and failed to elicit neurotoxic symptoms in experimental animals and oedema in the foot pads of mice. Also, its myotoxic and anticoagulant potencies were decreased significantly.

Item Type: Article
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Users 23 not found.
Date Deposited: 02 May 2021 03:38
Last Modified: 12 Jul 2022 09:38
URI: http://eprints.uni-mysore.ac.in/id/eprint/16240

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