Interaction between new neoglycoproteins and thed-Man/l-fuc receptor of rabbit alveolar macrophages |
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Authors: | Yukihide Ohsumi Victor J Chen Sau-Chi Bettyyan Finn Wold Yuan Chuan Lee |
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Affiliation: | (1) Department of Biology and the McCollum-Pratt Institute, Johns Hopkins University, 21218 Baltimore, MD, USA;(2) Department of Biochemistry and Molecular Biology, The University of Texas Medical School, 77225 Houston, TX, USA |
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Abstract: | New types of neoglycoproteins, -caseins coupled with ovalbumin-derived asparagine oligosaccharides (AO), aspartate aminotransferase-phosphopyridoxylated AO complex (AAT-PG), and streptavidin-biotinylated AO complex (SA-BAO), were tested for their inhibitory effect on binding of bovine serum albumin derivatized with thiomannoside, Man-AI-BSA [Lee YC, Stowell CP, Krantz MJ (1976) Biochemistry 15:3956–63] by rabbit alveolar macrophages. The -casein derivatives and the AAT-PG complex increased binding affinity as the number of oligosaccharide chains attached was increased. Their inhibitory potencies were closely related to those of the Man-Al-BSA derivatives [Hoppe CA, Lee YC (1983) J Biol Chem 258:14193–99] on the basis of terminal mannose density. The SA-BAO complex containing three AO chains gave stronger inhibitory potency than the -casein derivative with three AO residues, suggesting that proper orientation of the oligosaccharides on the protein can affect the receptor-ligand interaction.Abbreviations BSA bovine serum albumin - Man43-BSA BSA derivative containing on average 43 residues of Man linked through an amidino-linkage [7] - AO asparagine oligosaccharide (Man5-GlcNAc2-Asn) from ovalbumin - AAT aspartate aminotransferase - PG phosphopyridoxylated AO - SA streptavidin - BAO biotinylated AO |
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Keywords: | neoglycoprotein alveolar macrophage receptor |
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