Binding of D-galactose-terminated ligands to rabbit asialoglycoprotein receptor.

The binding affinities of a series of D-galactose-terminated glycerol glycosides and oligosaccharides for the asialoglycoprotein receptor isolated from rabbit liver were determined in vitro using a radioreceptor-inhibition assay with 125I-asialoorosomucoid. The relative affinities of the synthetic ligands increased with the number of exposed D-galactose termini. Of the compounds examined, 1,2,3-tri-O-beta-lactosylglycerol associated with the greatest affinity (estimated Kd = 7.97 x 10(-5) M). Examination of the affinities of the synthetic series indicated that both the number and propinquity of the D-galactose termini influenced the strength of the binding interactions.