| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
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| Autores: |
Pérez,A.V
Rucavado,A
Sanz,L
Calvete,J.J
Gutiérrez,J.M
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| Data: |
2008-01-01
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| Ano: |
2008
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| Palavras-chave: |
Snake venom
Bothrops asper
Serine proteinase
Thrombin-like serine proteinase
Defibrin(ogen)ation
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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.
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| Tipo: |
Info:eu-repo/semantics/other
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000100003
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X2006005000189
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.41 n.1 2008
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| Direitos: |
info:eu-repo/semantics/openAccess
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