The effects of acetylation on the binding region of cartilage proteoglycans to hyaluronic acid.
Proteoglycans in cartilage are found as aggregates and as monomers. Evidence has been obtained indicating that hyaluronic acid, normally present in this tissue, binds together monomers into large molecular weight aggregates. In this investigation, the interacting region of the protein backbone has been studied. The results unequivocally demonstrated that the epsilon amino groups of lysine are involved in hyaluronic acid binding to proteoglycans and that their blocking by acetylation either prevents reaggregation or disaggregates the high mol.w aggregates.
D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D002356:Cartilage; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D006820:Hyaluronic Acid; D008239:Lysine; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D011509:Proteoglycans; D014783:Viscosity
D046911:Macromolecular Substances; D011509:Proteoglycans; D006820:Hyaluronic Acid; D008239:Lysine