Characterization of an Agrobacterium tumefaciens lectin. |
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Authors: | C Depierreux H C Kang B Guérin M Monsigny F Delmotte |
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Affiliation: | Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France. |
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Abstract: | An Agrobacterium tumefaciens suspension induces a strong agglutination of aldehyde-fixed pig erythrocytes at pH 5.0. The agglutination is inhibited by some polysaccharides, such as fucoidin, and also when the pH is raised to 7.0. Lectins (sugar-binding proteins) associated with the bacterial cell wall of A. tumefaciens strain 84.5 were directly evidenced by spectrofluorimetry using fluoresceinylated neoglycoproteins. The specific binding of the fluorescein-labelled neoglycoprotein bearing alpha-L-fucoside residues was also optimal at pH 5.0. A lectin was purified by affinity chromatography on agarose substituted with alpha-L-fucopyranoside. Furthermore, the haemagglutination activity of this lectin was inhibited by polysaccharides isolated from poplar leaves. |
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