Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features.
A series of synthetic oligosaccharides, resembling natural N-acetyllactosamine type glycans, were tested for their ability to inhibit the binding of labeled ligand to the mammalian hepatic lectin on rabbit hepatocytes at 2 degrees C. A dramatic hierarchy of inhibitory potency (tetraantennary greater than triantennary much greater than biantennary much greater than monoantennary) could be demonstrated. The range of concentration required for 50% inhibition of labeled ligand binding extended from approximately 1 mM, for the monoantennary oligosaccharides, to approximately 1 nM for triantennary oligosaccharides, even though the absolute Gal concentration increased only 3-fold. It was found that the number of Gal residues/cluster and their branching mode are major determinants of binding affinity of ligands to the hepatic lectin on the surface of hepatocytes.
D000818:Animals; D001667:Binding, Competitive; D002240:Carbohydrate Sequence; D002462:Cell Membrane / Q000378:metabolism; D006020:Glycopeptides; D007700:Kinetics; D037102:Lectins; D008099:Liver / Q000276:immunology*; D009844:Oligosaccharides; D011817:Rabbits; D013329:Structure-Activity Relationship
D006020:Glycopeptides; D037102:Lectins; D009844:Oligosaccharides