Beta-Elimination and sulfite addition reaction of chondroitin sulfate peptidoglycan and the peptide structure of the linkage region.
Pronase digestion of bovine tracheal cartilage yielded acid mucopolysaccharide - peptide complexes which were fractionated by chromatography on Dowex 1(C1-). A major fraction was eluted with 1.5 M NaC1 and presumed to by chondroitin  sulfate A-peptidoglycan by cellulose acetate electrophoresis. Alkaline beta-elimination and sulfite addition reaction of this fraction yielded cysteic acid-containing peptides, two of which were obtained in an homogeneous state. The sequence determination of these two made it possible to remodel their original structures as Leu-Pro-Ser-Gly-Glu-Gly-Pro-Glu and Leu-Pro-Ser-Gly-Glu, where the serine residues carried polysaccharide chains. Together with the reported data on the polysaccharide-protein linkage region, the present result suggests that the -Ser-Gly- sequence is a minimum requisite for the glycosylation of serine residues in the protein core of various proteoglycans.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002356:Cartilage / Q000032:analysis; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D002809:Chondroitin Sulfates; D009928:Organ Specificity; D010457:Peptidoglycan / Q000032:analysis; D011485:Protein Binding; D011509:Proteoglycans / Q000032:analysis; D013447:Sulfites; D014132:Trachea
D000596:Amino Acids; D010457:Peptidoglycan; D011509:Proteoglycans; D013447:Sulfites; D002807:Chondroitin; D002809:Chondroitin Sulfates