Background: Erythrina corallodendron lectin (ECorL) is one of the potent applied lectins. In previous studies, the carbohydrate specificities of this lectin were limited to monosaccharides, simple oligosaccharides and several clusters. However, the polyvalent factor has not been investigated.
View Article and Find Full Text PDFPrevious studies on the carbohydrate specificities of Erythrina cristagalli lectin (ECL) were mainly limited to analyzing the binding of oligo-antennary Galbeta1-->4GlcNAc (II). In this report, a wider range of recognition factors of ECL toward known mammalian ligands and glycans were examined by enzyme-linked lectinosorbent and inhibition assays, using natural polyvalent glycotopes, and a glycan array assay. From the results, it is shown that GalNAc was an active ligand, but its polyvalent structural units, in contrast to those of Gal, were poor inhibitors.
View Article and Find Full Text PDFBackground: Ricin (RCA2 or RCA60) is a highly toxic heterodimeric protein found in the seeds of the castor plant Ricinus communis. It is a potential biohazard. In the present study, the fine specificity of ricin was defined.
View Article and Find Full Text PDFGalectins, a family of beta-galactoside-specific endogenous lectins, are involved in regulating diverse activities such as proliferation/apoptosis, cell-cell (matrix) interaction and cell migration. It is presently unclear to what extent the carbohydrate fine specificities of the combining sites of mammalian galectins overlap. To address this issue, we performed an analysis of the carbohydrate-recognition domain (CRD-I) near the N-terminus of recombinant rat galectin-4 (G4-N) by the biotin/avidin-mediated microtitre plate lectin-binding assay with natural glycoproteins (gps)/polysaccharide and by the inhibition of galectin-glycan interactions with a panel of glycosubstances.
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