Data/hora: 07/06/2024 11:31:53

Provedor de dados: 	52	
País: 	Brazil	
Título: 	Isolation and partial characterization of a D-galactose-binding lectin from the latex of Synadenium carinatum	
Autores: 	Souza,Maria Aparecida; Amâncio-Pereira,Francielle; Cardoso,Cristina Ribeiro Barros; Silva,Adriano Gomes da; Silva,Edmar Gomes; Andrade,Lívia Resende; Pena,Janethe Deolina Oliveira; Lanza,Henrique; Afonso-Cardoso,Sandra Regina.	
Data: 	2005-09-01	
Ano: 	2005	
Palavras-chave: 	D-Galactose-binding; Lectin; Latex; Synadenium carinatum.	
Resumo: 	A lectin from the latex of Synadenium carinatum was purified by affinity chromatography on immobilized-D-galactose-agarose and shown to be a potent agglutinin of human erythrocytes. The haemagglutination of human red cells was inhibited by 3.0 mM N-acetyl-D-galactopyranoside, 6.3 mM methyl-beta-D-galactopyranoside, 50 mM methyl-alpha-D-galactopyranoside and 50 mM D-fucose but not by L-fucose, demonstrating an anomeric and a conformational specificity. According to SDS-PAGE analysis, the lectin appeared to be a glycoprotein composed of two polypeptide chains of ca. 28 and 30 kDa, but size exclusion chromatography (Sephadex G-100) and native PAGE revealed a protein of apparent molecular weight 120 - 130 kDa made up of 28 and 30 kDa subunits. The lectin was stable in the range pH 6 - 9, and 4 - 56ºC. The N-terminal sequence of the 30 kDa subunit contained the conserved consensus sequence GPN observed in other D-galactose-binding lectins found in latex of members of the Euphorbiaceae.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000600005	
Editor: 	Instituto de Tecnologia do Paraná - Tecpar	
Relação: 	10.1590/S1516-89132005000600005	
Formato: 	text/html	
Fonte: 	Brazilian Archives of Biology and Technology  v.48 n.5 2005	
Fonte: 	info:eu-repo/semantics/openAccess