Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
Braz. j. med. biol. res
;
41(1): 12-17, Jan. 2008. graf
Article
in English
| LILACS
| ID: lil-469981
ABSTRACT
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 percent 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.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Blood Coagulation
/
Serine Endopeptidases
/
Coagulants
/
Bothrops
/
Crotalid Venoms
Limits:
Animals
Country/Region as subject:
Central America
/
Costa Rica
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
2008
Type:
Article
/
Project document
Affiliation country:
Costa Rica
/
Spain
Institution/Affiliation country:
Instituto de Biomedicina de Valencia/ES
/
Universidad de Costa Rica/CR
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