Beta-Elimination and sulfite addition reaction of chondroitin sulfate peptidoglycan and the peptide structure of the linkage region.

Biochimica Et Biophysica Acta
M Isemura, T Ikenaka

Abstract

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.

Citations

Jan 1, 1984·The International Journal of Biochemistry·Y Tanaka, I Takazono
Jul 15, 1977·Experientia·M Isemura, T Ikenaka
May 2, 1979·Clinica Chimica Acta; International Journal of Clinical Chemistry·M IsemuraY Sato

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