Binding of d-galactose-terminated ligands to rabbit asialoglycoprotein receptor

• Published in: Carbohydrate research 1994-02, Vol.254, p.257-268
• Main Authors: Krebs, Anita, Depew, William T., Szarek, Walter A., Hay, George W., Hronowski, Lucjan J.J.
• Format: Article
• Language: English
• Subjects: Animals; Asialoglycoprotein Receptor; Asialoglycoproteins - metabolism; Binding, Competitive; Biological and medical sciences; Carbohydrate Conformation; Carbohydrate Sequence; Cell receptors; Cell structures and functions; Fundamental and applied biological sciences. Psychology; Galactose; Iodine Radioisotopes; Kinetics; Ligands; Liver - metabolism; Miscellaneous; Molecular and cellular biology; Molecular Sequence Data; Oligosaccharides - chemistry; Oligosaccharides - metabolism; Oligosaccharides - pharmacology; Orosomucoid - analogs & derivatives; Orosomucoid - metabolism; Rabbits; Receptors, Cell Surface - drug effects; Receptors, Cell Surface - isolation & purification; Receptors, Cell Surface - metabolism
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/0008-6215(94)84258-2

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.