Abstract
The carbohydrate-binding specificity of a novel plant lectin isolated from the seeds of Tetracarpidium conophorum (Nigerian walnut) has been studied by quantitative hapten inhibition assays and by determining the behavior of a number of oligosaccharides and glycopeptides on lectin-Sepharose affinity columns. The Tetracarpidium lectin shows preference for simple, unbranched oligosaccharides containing a terminal Gal beta 1----4GlNAc sequence over a Gal beta 1----3GlcNAc sequence and substitution by sialic acid or fucose of the terminal galactose residue, the subterminal N-acetylglucosamine or more distally located sugar residues of oligosaccharides reduce binding activity. Branched complex-type glycans containing either Gal beta 1----4GlcNAc or Gal beta 1----3GlcNAc termini bind with higher affinity than simpler oligosaccharides. The lectin shows highest affinity for a tri-antennary glycan carrying Gal beta 1----4GlcNAc substituents on C-2 and C-4 of Man alpha 1----3 and C-2 of Man alpha 1----6 core residues. Bi- and tri-glycans lacking this branching pattern bind more weakly. Tetra-antennary glycans and mono- and di-branched hybrid-type glycans also bind weakly to the immobilized lectin. Therefore, Tetracarpidium lectin complements the binding specificities of well-known lectins such as Datura stramonium agglutinin, Phaseolus vulgaris agglutinin, and lentil lectin and will be a useful additional tool for the identification and separation of complex-type glycans.
Highlights
The carbohydrate-binding specificity of a novel In this papewr e describe in detail the carbohydrate-binding plant lectin isolated from the seeds of Tetracarpidium properties of T. conophorum agglutinin (TCA),' as examined conophorum(Nigerian walnut) has been studied by by hapten inhibition experiments andby affinity chromatogquantitative hapten inhibition assays and by determining the behavior of a number of oligosaccharides and glycopeptides on lectin-Sepharose affinity columns
The results obtained in this study indicate that TCA is a useful addition to thelist of galactose-binding lectins used for identification and fractionationof glycopeptidesand oligosacweakly to TCA-Sepharose (Table 111), all of the bi- charides
The dataderived from hapten inhibition assays and antennary complex-type fraction is fully galactosylated
Summary
The carbohydrate-binding specificity of a novel In this papewr e describe in detail the carbohydrate-binding plant lectin isolated from the seeds of Tetracarpidium properties of T. conophorum agglutinin (TCA),' as examined conophorum(Nigerian walnut) has been studied by by hapten inhibition experiments andby affinity chromatogquantitative hapten inhibition assays and by determining the behavior of a number of oligosaccharides and glycopeptides on lectin-Sepharose affinity columns. Glycopeptides obtained from either asialofetuin asialotransferrin are not available for binding to TCA under or asialotransferrin were several hundred fold more inhibitory the conditions used, due either to shielding by the protein than simple unbranched oligosaccharides
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