The alkali labile linkage between keratan sulphate and protein

J. J. Hopwood, H. C. Robinson

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


Keratan sulphate was isolated from adult intervertebral disc in 90% yield by sequential digestion of the whole tissue with papain, Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond between N acetylgalactosamine and threonine and produced, by an alkali catalyzed 'peeling' reaction, an unsaturated derivative of N acetylgalactosamine which reacted as a chromogen in the Morgan Elson reaction, but remained covalently bonded to the keratan sulphate chain. This derivative was reduced and labelled by alkaline NaB3H4. The substituent at position 3 of N acetylgalactosamine in the keratan sulphate/protein linkage was identified as a disaccharide, N acetylneuraminylgalactose, which was isolated from the reaction mixture after alkali treatment.

Original languageEnglish
Pages (from-to)57-69
Number of pages13
JournalBiochemical Journal
Issue number1
Publication statusPublished or Issued - 1974

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this