Abstract
A sensitive, accurate, and efficient biosensor analysis using surface plasmon resonance (SPR) spectroscopy was used for delineating the molecular interaction between rabbit liver asialoglycoprotein receptors (ASGPR) and glycosylated proteins. Isolated rabbit liver ASGPR obtained by affinity column chromatography was dissolved in buffer solution containing TritonX-100 and immobilized on the SPR sensor chip by amine coupling. The SPR study demonstrated that the association rate constants ( k a) of galactosylated proteins with ASGPR are dependent on the number of galactose residues, while the dissociation rate constants ( k d) are influenced not only by the surface density of the galactose moieties but also by their steric configuration. In addition, it was demonstrated that d-fucosylated BSA had a higher binding affinity to ASGPR than Gal-BSA, when the degree of sugar modification was equivalent.
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