• 15 May 1989
    • journal article
    • research article
    • Vol. 264  (14) , 7962-7969
Abstract
The interaction of the bovine cation-independent mannose 6-phosphate receptor with a variety of phosphorylated ligands has been studied using equilibrium dialysis and immobilized receptor to measure ligand binding. The dissociation constants for mannose 6-phosphate, pentamannose phosphate, bovine testes .beta.-galactosidase, and a high mannose oligosaccharide with two phosphomonoesters were 7 .times. 10-6 M, 6 .times. 10-6 M, 2 .times. 10-8 M, and 2 .times. 10-9 M, and the mol of ligand bound/mol of receptor monomer were 2.17, 1.85, 0.9, and 1.0, respectively. We conclude that the cation-independent mannose 6-phosphate receptor has two mannose 6-phosphate-binding sites/polypeptide chain.

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