Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor.

摘要: The interactions of the bovine cation-dependent mannose 6-phosphate receptor with monovalent and divalent ligands have been studied by equilibrium dialysis. This appears to be a homodimer or tetramer. Each mole monomer bound 1.2 mol ligands, pentamannose phosphate Kd values 8 X 10(-6) M 6 M, respectively 0.5 ligand, high oligosaccharide two phosphomonoesters, 2 10(-7) M. When Mn2+ was replaced EDTA in dialysis buffer, for 2.5 10(-5) By measuring affinity cation-independent receptors variety analogs, we conclude that 2-hydroxyl each contribute approximately 4-5 kcal/mol Gibb's free energy binding reaction. Neither interact substantially anomeric oxygen 6-phosphate. differ displays no detectable N-acetylglucosamine 1'-(alpha-D-methylmannopyranose 6-monophosphate) whereas this ligand binds poor, but readily measurable about 0.1 mM. spacing 6-phosphate-binding sites relative other may also receptors.