Data/hora: 09/06/2024 12:25:53

Provedor de dados: 	80	
País: 	Brazil	
Título: 	Purification and partial characterization of phospholipases A2 from Bothrops asper (barba amarilla) snake venom from Chiriguaná (Cesar, Colombia)	
Autores: 	Ramírez-Avila,J.; Quevedo,B. E.; López,E.; Renjifo,J. M.	
Data: 	2004-01-01	
Ano: 	2004	
Palavras-chave: 	Phospholipase; Isoenzymes; Snake; Venom; Bothrops asper; Colombia.	
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.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992004000300005	
Editor: 	Centro de Estudos de Venenos e Animais Peçonhentos	
Relação: 	10.1590/S1678-91992004000300005	
Formato: 	text/html	
Fonte: 	Journal of Venomous Animals and Toxins including Tropical Diseases  v.10 n.3 2004	
Fonte: 	info:eu-repo/semantics/openAccess