Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Ability Of Rabbit Antiserum Against Crotapotin To Neutralize The Neurotoxic, Myotoxic And Phospholipase A2 Activities Of Crotoxin From Crotalus Durissus Cascavella Snake Venom.
Author: Beghini, Daniela G
Damico, Daniela C S
da Cruz-Höfling, Maria Alice
Rodrigues-Simioni, Léa
Delatorre, Maria Carolina
Hyslop, Stephen
Marangoni, Sérgio
Abstract: The toxicity of crotoxin, the major toxin of Crotalus durissus terrificus (South American rattlesnake) venom, is mediated by its basic phospholipase A(2) (PLA(2)) subunit. This PLA(2) is non-covalently associated with crotapotin, an acidic, enzymatically inactive subunit of the crotoxin complex. In this work, rabbit antiserum raised against crotapotin purified from Crotalus durissus cascavella venom was tested for its ability to neutralize the neurotoxicity of this venom and its crotoxin in vitro. The ability of this antiserum to inhibit the enzymatic activity of the crotoxin complex and PLA(2) alone was also assessed, and its potency in preventing myotoxicity was compared with that of antisera raised against crotoxin and PLA(2). Antiserum to crotapotin partially neutralized the neuromuscular blockade caused by venom and crotoxin in electrically stimulated mouse phrenic nerve-hemidiaphragm preparations and prevented the venom-induced myotoxicity, but did not inhibit the enzymatic activity of crotoxin and purified PLA(2). In contrast, previous findings showed that antisera against crotoxin and PLA(2) from C. d. cascavella effectively neutralized the neuromuscular blockade and PLA(2) activity of this venom and its crotoxin. The partial neutralization of crotoxin-mediated neurotoxicity by antiserum to crotapotin probably reduced the binding of crotoxin to its receptor following interaction of the antiserum with the crotapotin moiety of the complex.
Subject: Animals
Crotalid Venoms
Electric Stimulation
In Vitro Techniques
Phospholipases A2
Protein Binding
Citation: Toxicology In Vitro : An International Journal Published In Association With Bibra. v. 22, n. 1, p. 240-8, 2008-Feb.
Rights: fechado
Identifier DOI: 10.1016/j.tiv.2007.08.007
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_17920236.pdf810.19 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.