Data/hora: 10/06/2024 15:17:42

Provedor de dados: 	88	
País: 	Brazil	
Título: 	Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. &amp;amp; Hommers.	
Autores: 	OLIVEIRA,STÉLIO R.M.; NASCIMENTO,ANTONIA E.; LIMA,MARIA E.P.; LEITE,YÁSKARA F.M.M.; BENEVIDES,NORMA M.B.	
Data: 	2002-12-01	
Ano: 	2002	
Palavras-chave: 	Agglutinin; Algae; Lectin; Pterocladiella capillacea; Purification.	
Resumo: 	A lectin present in the marine red alga Pterocladiella capillacea was purified and characterised by extraction of soluble proteins (crude extract) in 20 mM Tris-HCl buffer, pH 7.5. Among the analysed erythrocytes (human blood group A, B and O and the animals ox, goat, chicken and rabbit) the lectin agglutinated specifically rabbit erythrocytes. The hemagglutinating activity assay showed that the lectin was not dependent on divalent cations and was shown to be inhibited by the glycoproteins avidin and mucin. The purification procedure was conduced by precipitation of the crude extract with 80% saturation ammonium sulfate (F0/80) followed by affinity chromatography on guar-gum column. The lectin of P. capillacea was purified 14.5 fold and had a recovery of 27.4% of the original total specific activity present in the crude extract. The absence of carbohydrate suggested that the lectin is not a glycoprotein. The molecular mass of P. capillacea lectin, determined by gel filtration, was 5.8 kDa. SDS-PAGE in the presence of ß-mercaptoethanol gave one band, indicating that the native lectin is a monomeric protein. The activation energy of denaturation process (D G') was calculated to be 106.87 kJ . mol-1 at 70 ºC.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84042002012000003	
Editor: 	Sociedade Botânica de São Paulo	
Relação: 	10.1590/S0100-84042002012000003	
Formato: 	text/html	
Fonte: 	Brazilian Journal of Botany  v.25 n.4 2002	
Fonte: 	info:eu-repo/semantics/openAccess