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Distler JJ, Guo JF, Jourdian GW, et al. The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides. J Biol Chem. 1991;266(32):21687-92
Distler, J. J., Guo, J. F., Jourdian, G. W., Srivastava, O. P., & Hindsgaul, O. (1991). The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides. The Journal of biological chemistry, 266(32), 21687-92.
Distler, J J, et al. "The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides." The Journal of biological chemistry vol. 266,32 (1991): 21687-92.
Distler JJ, Guo JF, Jourdian GW, Srivastava OP, Hindsgaul O. The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides. J Biol Chem. 1991 Nov 15;266(32):21687-92. PMID: 1657978.
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Elsevier Science

J Biol Chem. 1991 Nov 15;266(32):21687-92.

The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides.

The Journal of biological chemistry

J J Distler, J F Guo, G W Jourdian, O P Srivastava, O Hindsgaul

Affiliations

  1. Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109.

PMID: 1657978
Free Article

Abstract

A series of chemically synthesized oligomannosides that contain mannose 6-phosphate residues were utilized as inhibitors of the binding of beta-galactosidase to high (CI-MPR, 215 kDa) and low (CD-MPR, 41-46 kDa) molecular mass mannose 6-phosphate receptor from bovine testes in order to probe the specificity of each receptor. Mannobioside phosphorylated in the terminal position and linked alpha(1,2) was a 6-fold better inhibitor than the corresponding alpha(1,3)- and alpha (1,6)-linked isomers. Inhibition observed with a monophosphorylated alpha(1,2)-linked mannotrioside was approximately 6-fold greater than that with the corresponding mannobioside. Penultimate glycosidic linkages of the oligomannosides played little or no role in the inhibition of binding of ligand to the receptors. Monophosphorylated oligomannosides containing phosphomonoester groups on penultimate mannose residues were not inhibitors. Binding inhibition observed for biantennary oligomannosides with phosphate on terminal mannose residues of either alpha(1,3) or alpha(1,6) chains closely approximated the values obtained with analogous trimannosides. A biantennary oligomannoside on which each antennary chain contained a terminal phosphate exhibited approximately an 8-fold greater inhibition than monophosphorylated compounds. Although the receptors exhibited similar relative specificities for phosphomonoesters, phosphodiesters did not inhibit binding of ligand to CD-MPR and only weakly inhibited binding to CI-MPR.

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