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, Aida Verónica, Rucavado Romero, Alexandra, Sanz, Libia, Calvete Chornet, Juan José, Gutiérrez, José María
Formato: artículo original
Fecha de Publicación:2008
Descripción: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..
País:Kérwá
Institución:Universidad de Costa Rica
Repositorio:Kérwá
OAI Identifier:oai:https://www.kerwa.ucr.ac.cr:10669/29337
Acceso en línea:http://www.bjournal.com.br/index.php?option=com_jresearch&view=publication&task=show&id=10377
https://hdl.handle.net/10669/29337
Access Level:acceso abierto
Palabra clave:Bothrops Asper
Serine Proteinase
Thrombin-like serine proteinase
Defibrin(ogen)ation
Snake venom