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Biochemistry (Mosc) ; 74(3): 329-35, 2009 Mar.
Article in English | MEDLINE | ID: mdl-19364328

ABSTRACT

A lectin was isolated from the roots of Sesbania aculeata. This is a glucose specific lectin having 39 kDa subunit molecular weight. The expression of this lectin was found to be developmentally regulated and observed to be the highest in the second week. The lectin was purified by affinity chromatography using Sephadex G-50 and found to have 28% homology with Arabidopsis thaliana lectin-like protein (accession No. CAA62665). The lectin binds with lipopolysaccharide isolated from different rhizobial strains indicating the plants interaction with multiple rhizobial species.


Subject(s)
Plant Lectins/metabolism , Plant Roots/metabolism , Sesbania/metabolism , Amino Acid Sequence , Animals , Carbohydrates/analysis , Chromatography, Affinity , Electrophoresis, Gel, Two-Dimensional , Electrophoresis, Polyacrylamide Gel , Hemagglutination Tests , Lipopolysaccharides/chemistry , Lipopolysaccharides/metabolism , Molecular Sequence Data , Molecular Weight , Plant Lectins/chemistry , Plant Lectins/physiology , Protein Binding , Rabbits , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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