Self-aggregation of bovine skin proteodermatan sulphate promoted by removal of the three N-linked oligosaccharides

Progressive digestion of native bovine skin proteodermatan sulphate with glycopeptidase F (EC. 3.2.2.18), followed by electrophoresis and affinity-blotting with concanavalin A, demonstrated the presence of three N-linked oligosaccharide chains on the protein core. These oligosaccharides were localized to the C-terminal portion of the protein core. Proteodermatan sulphate purified after removal of the oligosaccharides exhibited an altered circular dichroism spectrum and apparently enhanced thermal stability which were explained by the finding that it had aggregated. The aggregates could be partially dissociated by urea. Aggregation could also be demonstrated without intervening preparative steps between digestion with glycopeptidase-F and electrophoresis. Oligosaccharide-free proteodermatan sulphate retained its ability to inhibit fibril formation from monomeric collagen but showed a tendency to self-aggregate in solution. These results suggest a role for the oligosaccharides of proteodermatan sulphate in maintaining the molecule in a predominantly monomeric form in the tissue, thus indirectly promoting its interaction with collagen.