Consulta: subjectFacets:"Defibrin(ogen)ation"
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Data/hora: 18/06/2024 12:25:56

Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
Provedor de dados: 56
Autores: 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