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| 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. |
| 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... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: D-Galactose-binding; Lectin; Latex; Synadenium carinatum. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000600005 |
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