Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BJMBR (1) J. Venom. Anim. Toxins incl. Trop. Dis. (1) Autor Barraviera,B (1) Barraviera,SRCS (1) Barros,LC (1) Calvete,J.J (1) Costa,FL (1) Ferreira Junior,RS (1) Fuly,AL (1) Gallacci,M (1) Giglio,JR (1) Gutiérrez,J.M (1) Pérez,A.V (1) Rodrigues,VM (1) Rucavado,A (1) Sanz,L (1) Soares,AM (1) Thomazini-Santos,IA (1) Mais... Palavra-chave Serine proteinase (2) Bothrops asper (1) Coagulant activity (1) Crotalus durissus terrificus (1) Defibrin(ogen)ation (1) Gyroxin (1) Neurotoxicity (1) Snake venom (1) Thrombin-like serine proteinase (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Info:eu-repo/semantics/other (1) Ano 2011 (1) 2008 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última 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 Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper BJMBR Pérez,A.V; Rucavado,A; Sanz,L; Calvete,J.J; Gutiérrez,J.M. A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose and ion-exchange chromatography on DEAE-Sepharose. The enzyme accounts for approximately 0.13% of the venom dry weight and has a molecular mass of 32 kDa as determined by SDS-PAGE, and of 27 kDa as determined by MALDI-TOF mass spectrometry. Its partial amino acid sequence shows high identity with snake venom serine proteinases and a complete identity with a cDNA clone previously sequenced from this species. The N-terminal sequence of the enzyme is VIGGDECNINEHRSLVVLFXSSGFL CAGTLVQDEWVLTAANCDSKNFQ. The enzyme induces clotting of plasma... Tipo: Info:eu-repo/semantics/other Palavras-chave: Snake venom; Bothrops asper; Serine proteinase; Thrombin-like serine proteinase; Defibrin(ogen)ation. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000100003 Registros recuperados: 2 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco