Purification and partial characterization of phospholipases A2 from Bothrops asper (barba amarilla) snake venom from Chiriguaná (Cesar, Colombia)
J. venom. anim. toxins incl. trop. dis
;
10(3): 242-259, 2004. ilus, tab, graf
Artículo
en Inglés
| LILACS
| ID: lil-383135
RESUMO
Components with phospholipase A2 activity were isolated by gel filtration and cationic exchange chromatography from the venom of Bothrops asper snakes from Chiriguaná, Colombia (9°22´N; 73°37´W). Five fractions were obtained by the gel filtration, and PLA2 activity was found in fraction 3 (F3). In the cationic exchange chromatography, F3 showed eight components with PLA2 activity. Six of these components appeared as one band in polyacrylamide gel electrophoresis (SDS-PAGE). Fractions II and VII exhibited an optimal activity at pH 9 and 52ºC. The optimum calcium concentration for fraction II was 48 mM and for fraction VII, 384 mM. Both fractions showed thermal stability. Fraction II was stable at pH values between 2.5 and 9, and fraction VII, between 2.5 and 8. The Michaelis Menten constant (K M) was 3.5x10-3 M for fraction II and 1.6x10-3 M for fraction VII. The molecular weight was 16,000 Dalton for fraction II and 17,000 Dalton for fraction VII. Both isoenzymes did not show any toxic activity (DL50) at 5.3 and 4 µg/g. The two fractions showed different kinetic constant (K M), calcium requirement, and substrate specificity for haemolytic activity.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Fosfolipasas A
/
Venenos de Crotálidos
Límite:
Animales
País/Región como asunto:
America del Sur
/
Colombia
Idioma:
Inglés
Revista:
J. venom. anim. toxins incl. trop. dis
Asunto de la revista:
Toxicología
Año:
2004
Tipo del documento:
Artículo
/
Documento de proyecto
País de afiliación:
Colombia
Institución/País de afiliación:
National Institute of Health/CO
/
National University of Colombia/CO
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