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. 1974 Jul;141(1):57–69. doi: 10.1042/bj1410057

The alkali-labile linkage between keratan sulphate and protein

John J Hopwood 1,*, H Clem Robinson 1
PMCID: PMC1168049  PMID: 4281652

Abstract

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-catalysed `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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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