Literature DB >> 7940581

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

A S Babu1, T V Gowda.   

Abstract

The most basic phospholipase A2 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 micrograms/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 micrograms/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.

Entities:  

Mesh:

Substances:

Year:  1994        PMID: 7940581     DOI: 10.1016/0041-0101(94)90344-1

Source DB:  PubMed          Journal:  Toxicon        ISSN: 0041-0101            Impact factor:   3.033


  2 in total

1.  Biological and structural characterization of a new PLA2 from the Crotalus durissus collilineatus venom.

Authors:  M H Toyama; D O Toyama; Paulo P Joazeiro; E M Carneiro; L O S Beriam; L S Marangoni; A C Boschero
Journal:  Protein J       Date:  2005-02       Impact factor: 2.371

2.  Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics.

Authors:  Grazyna Faure; Veerabasappa T Gowda; Rachid C Maroun
Journal:  BMC Struct Biol       Date:  2007-12-06
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.