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	Provedor de dados BJMBR (1) Autor Calvete,J.J (1) Gutiérrez,J.M (1) Pérez,A.V (1) Rucavado,A (1) Sanz,L (1) Palavra-chave Bothrops asper (1) Defibrin(ogen)ation (1) Serine proteinase (1) Snake venom (1) Thrombin-like serine proteinase (1) Tipo do documento Info:eu-repo/semantics/other (1) Ano 2008 (1) País Brazil (1) Idioma Inglês (1)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 1 Primeira ... 1 ... Última 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: 1 Primeira ... 1 ... Última

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