Interaction of hyaluronectin with hyaluronic acid oligosaccharides.
Hyaluronic acid was digested by bovine testicular hyaluronidase, and oligomers were fractionated by gel permeation using AcA 202 Ultrogel, an acrylamide-agarose matrix. Oligosaccharides composed of from two to six disaccharide repeating units were isolated. Two nonasaccharides were prepared by enzymatic or chemical modification of the decasaccharide. Oligosaccharides were compared by a competitive inhibition in the enzyme-linked immunosorbent assay for their ability to inhibit the interaction of hyaluronectin (a hyaluronic acid-binding brain glycoprotein) with hyaluronic acid. Among these oligosaccharides, decasaccharides were the smallest fragments that strongly inhibited the interaction. Octasaccharides inhibited with 700-fold lower affinity than decasaccharides. Dodecasaccharides had the same effect as decasaccharides. Nonasaccharides obtained by beta-glucuronidase splitting of decasaccharides inhibited the interaction more than nonasaccharides prepared by an alkaline treatment.
Bertrand
P
P
Delpech
B
B
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002356:Cartilage / Q000378:metabolism; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D018960:Hyaluronan Receptors; D006820:Hyaluronic Acid / Q000378:metabolism*; D007106:Immune Sera / Q000276:immunology; D005779:Immunodiffusion; D009844:Oligosaccharides / Q000302:isolation & purification / Q000378:metabolism*; D011509:Proteoglycans / Q000378:metabolism; D011817:Rabbits / Q000276:immunology
D002352:Carrier Proteins; D018960:Hyaluronan Receptors; D007106:Immune Sera; D009844:Oligosaccharides; D011509:Proteoglycans; D006820:Hyaluronic Acid