Concanavalin A (ConA) isolated from jack bean (Can-
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چکیده
avalia ensiformis) belongs to the legume lectin family. Among the monosaccharides, methyl a-D-mannopyranoside (Me a-Man, see Chart) exhibits the most potent inhibitory effect on formation of the complex of ConA with dextran, and the mannotriose 3,6-di-O-(a-D-mannosyl)-a-D-mannoside was found to be the most potent oligosaccharide, being more potent than Me a-Man. Shinohara et al. examined the binding of ConA with glycosidase-treated fetuins containing the branched mannotriose moieties, which were immobilized in the chip of an optical biosensor utilizing the surface plasmon resonance (SPR) technique. Their results showed that the terminal mannotriose moiety of glucosaminidase-treated fetuin (aglucosaminofetuin) was most sensitive. Galactosidase-treated fetuin (agalactosylfetuin) and sialidase-treated fetuin (asialofetuin, ASF) having glycosylated non-terminal mannotriose moieties bound more weakly than aglucosaminofetuin to ConA. To understand the structural requirements of sugars for binding with ConA in biomembranes, we quantitatively analyzed the effects of various sugars on the dissociation of ConA from ASF using an optical biosensor system. As ASF does not interact with ConA tightly, the ASF–ConA system should be favorable for determination of the affinity of sugars for ConA. In fact, we found that our system is a good mode of interaction of sugars with ConA in biomembranes.
منابع مشابه
Recognition of septanose carbohydrates by concanavalin A.
The ability of the jack bean lectin concanavalin A (ConA) to bind seven membered ring (septanose) monosaccharides has been investigated by isothermal titration calorimetry (ITC) and saturation transfer difference (STD) NMR spectroscopy.
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Concanavalin A (ConA) is a well characterized and extensively used lectin accumulated in the protein bodies of jack bean cotyledons. ConA is synthesized as an inactive precursor proConA. The maturation of inactive proConA into biologically active ConA is a complex process including the removal of an internal glycopeptide and a C-terminal propeptide (CTPP), followed by a head-to-tail ligation of...
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Concanavalin A (ConA), one of the most studied plant lectins, is formed in jack bean (Canavalia ensiformis) seeds. ConA is synthesized as an inactive glycoprotein precursor proConA. Different processing events such as endoproteolytic cleavages, ligation of peptides and deglycosylation of the precursor are required to generate the different polypeptides constitutive of mature ConA. Among these e...
متن کاملThe Effects of Concanavalin A on Human Oral Epithelial Cell Staining Adhesion Under Various Conditions
Concanavlin A (ConA), a lectin found in jack-beans can bind to multiple sugars, as can cell receptors found on cheek epithelial cells and erythrocytes. By using horseradish peroxidase and hemagglutination, the effects of mannose and galactose on ConA binding were observed. Galactose had no effect on ConA but mannose bound with more affinity to ConA, competed negatively with the cell receptors, ...
متن کاملProtein-Carbohydrate Interaction III. Agar Gel-Diffusion Studies on the Interaction of Concanavalin A, a Lectin Isolated from Jack Bean, with Polysaccharidesl
Concanavalin A, a protein isolated from the jack bean (Canavalia ensijormis), has previously been shown to form a precipitate with glycogen and yeast mannan, and more recently with dextrans and amylopectin. Double-diffusion precipitation studies in agar gel have been found to afford a very sensitive and satisfactory method for investigating the interaction of concanavalin A with certain types o...
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