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• W2033202876 abstract "The hepatic asialoglycoprotein receptor is a hetero-oligomer composed of two homologous subunits. The specificity and affinity of ligand binding depends on the number and spatial arrangement of several galactose-binding sites within the receptor complex. Previous studies indicated that both subunits are required for high-affinity ligand binding, i.e. for the simultaneous interaction with three galactose residues within an N-linked glycan. However, we found that asialoorosomucoid (ASOR) and asialofetuin (ASF) bind to transfected COS-7 cells expressing subunit H1 in the absence of the second subunit H2. ASOR binding occurred with a dissociation constant of approximately 40 nM, approximately four-times higher than the Kd of ASOR binding to the hetero-oligomeric receptor. Normalized to the amount of H1 expressed, approximately 10–times fewer binding sites were produced by H1 alone. A glycopeptide with a single tri-antennary N-linked glycan purified from ASF bound to the hetero-oligomeric receptor, but did not bind detectably to HI-expressing COS-7 cells. H1 is thus unable to simultaneously recognize all three galactose residues in a glycan. From this, we conclude that, at a sufficiently high density of HI on the cell surface, high-affinity binding of ASOR and ASF is the result of two or more glycans interacting with H1 oligomers with low affinity in a bivalent manner." @default.
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• W2033202876 date "1995-05-01" @default.
• W2033202876 modified "2023-10-16" @default.
• W2033202876 title "High-Affinity Ligand Binding to Subunit HI of the Asialoglycoprotein Receptor in the Absence of Subunit H2" @default.
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• W2033202876 doi "https://doi.org/10.1111/j.1432-1033.1995.0207i.x" @default.
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