| Registro completo |
| Provedor de dados: |
BABT
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| País: |
Brazil
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| Título: |
Isolation and partial characterization of a D-galactose-binding lectin from the latex of Synadenium carinatum
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| 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
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| Data: |
2005-09-01
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| Ano: |
2005
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| Palavras-chave: |
D-Galactose-binding
Lectin
Latex
Synadenium carinatum
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| 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.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000600005
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| Editor: |
Instituto de Tecnologia do Paraná - Tecpar
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| Relação: |
10.1590/S1516-89132005000600005
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| Formato: |
text/html
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| Fonte: |
Brazilian Archives of Biology and Technology v.48 n.5 2005
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| Direitos: |
info:eu-repo/semantics/openAccess
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