Concanavalin A binding

Keenan, T. W., Franke, W. W. and Kartenbeck, J. 1974A. Concanavalin A binding by isolated plasma membranes and endomembranes from liver and mammary gland. Febs. Lett. 44, 274-278. 

Scott JK, Loganathan, Easley RB, Gong X, Goldstein IJ, A family of concanavalin A-binding peptides from a hexapeptide epitope library, Proc. Natl. Acad. Sci. USA, 89 5398-5402, 1992. 

Fig. 3. Concanavaline-A-induced, ligand-binding assay of various liposomal formulations. Concanavalin A solution (lOOgg/mL) was added to 0.2 mL of diluted liposomes formulations and absorbance at 550 nm was measured as a function of time. The data were subtracted from the blank experiment conducted without an addition of concanavalin A. Binding of the terminal mannose residues of the mannan to the ConA causes agglutination of the complex in solution resulting in an increase in turbidity. However, plain liposomes did prevent the binding of Con A as evidenced by the lower turbidity. The accessibility of the mannan to the liposomes is critical for in vivo cell binding...

Figure 2 Concanavalin A binding site showing metal chelation and hydrogen hond networks.

Fig. 7. (A) Concanavalin A binding and (B) non-binding di- and triantennary glycans from a-fetoprotein.

Other binding agents seem to have no effect on channel behavior. Concanavalin A binds to rat liver VDAC in the triton XIOO-solubilized form (4, 43). Antibodies against N. crassa VDAC inhibit VDAC insertion into planar membranes and bind to VDAC crystals in membranes, but do not affect channel behavior (44). These agents may interact with a surface domain on VDAC that does not respond to membrane potentials. 

The subcutaneous injection of a s-diamminedichlo-roplatinum(II) into ABD2F1 mice (8 mg/kg) resulted in alterations of size and surface structure of peritoneal macrophages and in a reduction of the mean number of their concanavalin A binding sites (Peschke et al. 1992). 

The major glycoproteins of the thymocyte plasma membrane which react with concanavalin A do not readily associate with other membrane proteins. It is possible that these concanavalin A-binding glycoproteins directly or indirectly modulate thymocyte function via their control of plasma membrane transport and/or permeability. 

A novel use of immobilized concanavalin A for the large-scale production of malaria merozoites has been described. Concanavalin A binds erythrocytes but not malarial parasites cells from infected blood were therefore specifically bound. On maturation of the schizonts they released merozoites which could be collected conveniently. 

Kanai M, Mortell KH, Kiessling LL (1997) Varying the size of multivalent ligands the dependence of concanavalin a binding on neoglycopolymer length. J Am Chem Soc 119(41) 9931-9932... 

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