Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom
1989; Elsevier BV; Volume: 27; Issue: 2 Linguagem: Inglês
10.1016/0041-0101(89)90136-0
ISSN1879-3150
AutoresS.R. Kasturi, T. Veerabasappa Gowda,
Tópico(s)Ion channel regulation and function
ResumoS. 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.
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