Concanavalin interactions with carbohydrates

Taken together, these results suggest that molecular recognition of the dodecapeptide by antibodies differs from its recognition by concanavahn A, and that the immunological cross-reactivity observed in some studies does not reflect structural mimicry. That molecular recognition by concanavalin A of carbohydrates and peptides differs has also been shown in structural studies. Here, the functional molecular mimicry observed with respect to different receptors should not be assumed to imply structural mimicry—the inter-molecular interactions may differ in each case. 

Goldstein L, Hollerman C, Smith EE. Protein-carbohydrate interaction. II. Inhibition studies on interaction of concanavalin A with polysaccharides. Biochemistry 1965, 4, 876-883. 

Iyer RN, Goldstein IJ. Quantitative studies on the interaction of concanavalin A, the carbohydrate-binding protein of the jack bean, with model carbohydrate-protein conjugates. Immunochemistry 1973 10 313-322. 

Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9].

Proline, 2-Oxoglutarate Dioxygenases.—Part of the enzymic activity was lost when the proline, 2-oxoglutarate dioxygenase from chicken embryos interacted with [ H-acetyl]concanavalin A, suggesting that the enzyme contains a carbohydrate component. ... 

Removal of polysaccharide contaminants from preparations of DNA by affinity chromatography Separation of membrane glycoproteins from rat-brain synaptic vesicles by affinity chromatography Studies of the interactions of the carbohydrate-binding sites on concanavalin A with adipocyte receptors... 

For many years this laboratory has been studying the interactions of concanavalin A (con A), a carbohydrate binding protein of considerable interest (X—4 ), with simple and complex carbohydrates (578)- It was established that compared to monosaccharides, oligosaccharides composed of a- (l- -2)-linked D-roannose units exhibited an enhanced affinity for con A (9). This increased affinity for con A was explained both in terms of an extended binding site (5,10) and a statistical mode (11). 

Polymer adsorption has also been adapted to QCM sensing whereby biofunctional thin films are adsorbed on the crystal surface with non-specific binding controlled by tuning of polymer composition. This approach proved successful as applied to carbohydrate-protein interaction by Matsuura et al. through adsorption of lactose bearing amphiphilic polymers on hydrophobic surfaces which then showed RCA12o and peanut lectin (PNA) affinity [33]. Carbohydrate surfaces prepared by photo insertion into an adsorbed polymer were tested by QCM and showed the predicted affinities [34] while in another example a covalently bound glycopolymer demonstrated Concanavalin A detection ability [35]. 

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