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The structure of the keratan sulphate attached to fibromodulin isolated from bovine tracheal cartilage, Oligosaccharides isolated following keratanase digestion.

Research output: Contribution to journalJournal article

Published
<mark>Journal publication date</mark>1/09/1994
<mark>Journal</mark>Biochemical Journal
Issue number2
Volume302
Number of pages7
Pages (from-to)417-423
<mark>State</mark>Published
<mark>Original language</mark>English

Abstract

The structure of the repeat region and chain caps of the N-linked keratan sulphate chains attached to bovine tracheal cartilage fibromodulin has been examined. The chains were fragmented by keratanase digestion, the resultant oligosaccharides isolated by strong anion-exchange chromatography, and their structures determined using high-field 1H-n.m.r. spectroscopy. The chains were found to possess the following general structure: [formula: see text] All of the capping oligosaccharides isolated terminate with alpha(2-3)-linked N-acetylneuraminic acid. No alpha(2-6)-linked N-acetylneuraminic acid chain terminators, nor any fucose, alpha (1-3)-linked to N-acetylglucosamine along the repeat region, were detected. This work demonstrates that the structure of the repeat region and chain caps of N-linked keratan sulphate attached to fibromodulin isolated from bovine tracheal cartilage is identical with that of O-linked keratan sulphate chains attached to aggrecan derived from non-articular cartilage.