Interactions of cartilage proteoglycans with hyaluronate. The role of the hyaluronate acetamido groups.
Hyaluronate oligomers were treated with anhydrous hydrazine in the presence of hydrazine sulfate to remove the N-acetyl groups. Complete deacetylation could not be achieved without extensive degradation of the oligosaccharide chain. Partially deacetylated oligomers exhibited decreased inhibition of cartilage proteoglycan-hyaluronate interaction as compared to the unreacted starting material; re-N-acetylation by reaction with acetic anhydride restored the inhibitory activity to a great extent. When the hydrazine-treated oligosaccharides were reacted with other acyl anhydrides, the inhibitory potency was restored to an extent which was inversely related to the size of the acyl group. Thus, for maximal interaction between hyaluronate and proteoglycan, the glucosamine residue of hyaluronate must be N-acylated with a minimally sized acyl group.
D000117:Acetylglucosamine / Q000032:analysis; D000818:Animals; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D006820:Hyaluronic Acid; D007700:Kinetics; D009300:Nasal Septum; D009844:Oligosaccharides; D011485:Protein Binding; D011509:Proteoglycans
D009844:Oligosaccharides; D011509:Proteoglycans; D006820:Hyaluronic Acid; D000117:Acetylglucosamine