Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors.

The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N-glycan chains, as well as their polyvalent forms in N-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian N-glycans, including the N-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by Molar Relative Potency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (M