Abstract
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 teh number of exposed d-galactose termini. Of the compounds examined, 1,2,3-tri- O-β-lactosylglycerol associated with the greatest affinity (estimated K d = 7.97 × 10 −5 M). Examination of the affinities of the syntetic series indicated that both the number and propinquity of the d-galactose termini influenced the strength of the binding interactions.
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