Binding of [1-13C]galactose-enriched hen ovalbumin to Erythrina cristagalli agglutinin as studied by 13C-NMR spectroscopy.
A study of the equilibrium binding of glycoproteins to lectins was undertaken using the titled compounds as a model system for such interactions. The binding of hen ovalbumin, enriched in galactose specifically 13C-labelled at C1, to Erythrina cristagalli agglutinin was studied by 13C-NMR spectroscopy. The lectin was shown to be bivalent for ovalbumin with an apparent estimated association constant, at infinite dilution, of about 10(4) M-1. The observed association is similar to that found for the corresponding disaccharide, Gal(beta 1-4)GlcNAc. The results strongly suggest that only the N-acetyllactosamine moiety in the carbohydrate side chain of galactose-enriched ovalbumin participates in the binding to the lectin with little, if any, interactions from other parts of either the side chain or the polypeptide backbone of ovalbumin.
D001665:Binding Sites; D002846:Chromatography, Affinity; D004895:Erythrina; D005690:Galactose / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D010047:Ovalbumin / Q000378:metabolism*; D037121:Plant Lectins; D010946:Plants, Medicinal
D037102:Lectins; D037121:Plant Lectins; C045629:erythrina lectin; D010047:Ovalbumin; D005690:Galactose