Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
Data(s) |
01/01/2008
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Resumo |
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 (minimum coagulant dose = 4.1 µg) and fibrinogen (minimum coagulant dose = 4.2 µg) in vitro, and promotes defibrin(ogen)ation in vivo (minimum defibrin(ogen)ating dose = 1.0 µg). In addition, when injected intravenously in mice at doses of 5 and 10 µg, it induces a series of behavioral changes, i.e., loss of the righting reflex, opisthotonus, and intermittent rotations over the long axis of the body, which closely resemble the `gyroxin-like' effect induced by other thrombin-like enzymes from snake venoms. |
Formato |
text/html |
Identificador |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000100003 |
Idioma(s) |
en |
Publicador |
Associação Brasileira de Divulgação Científica |
Fonte |
Brazilian Journal of Medical and Biological Research v.41 n.1 2008 |
Palavras-Chave | #Snake venom #Bothrops asper #Serine proteinase #Thrombin-like serine proteinase #Defibrin(ogen)ation |
Tipo |
journal article |