Abstract
New types of neoglycoproteins, β-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 β-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 β-casein derivative with three AO residues, suggesting that proper orientation of the oligosaccharides on the protein can affect the receptor-ligand interaction.
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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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Ohsumi, Y., Chen, V.J., Bettyyan, SC. et al. Interaction between new neoglycoproteins and thed-Man/l-fuc receptor of rabbit alveolar macrophages. Glycoconjugate J 5, 99–106 (1988). https://doi.org/10.1007/BF01048335
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DOI: https://doi.org/10.1007/BF01048335