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Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: Barros,LC; Soares,AM; Costa,FL; Rodrigues,VM; Fuly,AL; Giglio,JR; Gallacci,M; Thomazini-Santos,IA; Barraviera,SRCS; Barraviera,B; Ferreira Junior,RS.
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...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Gyroxin; Neurotoxicity; Coagulant activity; Crotalus durissus terrificus; Serine proteinase.
Ano: 2011
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004