Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
J. venom. anim. toxins incl. trop. dis
; 17(1): 23-33, 2011. graf
Artigo
em Inglês
| LILACS
| ID: lil-576879
Biblioteca responsável:
BR33.1
ABSTRACT
Gyroxin, a thrombin-like enzyme isolated from Crotalus durissus terrificus venom and capable of converting fibrinogen into fibrin, presents coagulant and neurotoxic activities. The aim of the present study was to evaluate such coagulant and toxic properties. Gyroxin was isolated using only two chromatographic steps - namely gel filtration (Sephadex G-75) and affinity (Benzamidine Sepharose 6B) - resulting in a sample of high purity, as evaluated by RP-HPLC C2/C18 and electrophoretic analysis that showed a molecular mass of 30 kDa. Gyroxin hydrolyzed specific chromogenic substrates, which caused it to be classified as a serine proteinase and thrombin-like enzyme. It was stable from pH 5.5 to 8.5 and inhibited by Mn²+, Cu²+, PMSF and benzamidine. Human plasma coagulation was more efficient at pH 6.0. An in vivo toxicity test showed that only behavioral alterations occurred, with no barrel rotation. Gyroxin was not able to block neuromuscular contraction in vitro, which suggests that its action, at the studied concentrations, has no effect on the peripheral nervous system.
Texto completo:
Disponível
Coleções:
Bases de dados internacionais
Base de dados:
LILACS
Assunto principal:
Trombina
/
Venenos de Crotalídeos
Limite:
Animais
Idioma:
Inglês
Revista:
J. venom. anim. toxins incl. trop. dis
Assunto da revista:
Toxicologia
Ano de publicação:
2011
Tipo de documento:
Artigo
País de afiliação:
Brasil
Instituição/País de afiliação:
Federal University of Uberlândia/BR
/
Fluminense Federal University/BR
/
São Paulo State University/BR
/
University of São Paulo/BR