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Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys J. Venom. Anim. Toxins incl. Trop. Dis.
Ghorbanpur,M; Zare Mirakabadi,A; Zokaee,F; Zolfagarrian,H; Rabiei,H.
Agkistrodon halys is one of several dangerous snake species in Iran. Among the most important signs and symptoms in patients envenomated by this snake is disseminated intravascular coagulation. A thrombin-like enzyme, called AH143, was isolated from Agkistrodon halys venom by gel filtration on a Sephadex G-50 column, ion-exchange chromatography on a DEAE-Sepharose and high performance liquid chromatography (HPLC) on a C18 column. In the final stage of purification, 0.82 mg of purified enzyme was obtained from 182.5 mg of venom. The purified enzyme showed a single protein band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), under reducing conditions, and its molecular mass was found to be about 30 kDa. AH143 revealed clotting...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Iranian snake; Venom; Agkistrodon halys; Serine protease; Chromatography; Coagulant activity.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992009000300005
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Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom J. Venom. Anim. Toxins incl. Trop. Dis.
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
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