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

Lauder, R. M. and Huckerby, T. N. and Nieduszynski, I. A. (1994) The structure of the keratan sulphate attached to fibromodulin isolated from bovine tracheal cartilage, Oligosaccharides isolated following keratanase digestion. Biochemical Journal, 302 (2). pp. 417-423. ISSN 0264-6021

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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.

Item Type:
Journal Article
Journal or Publication Title:
Biochemical Journal
Uncontrolled Keywords:
/dk/atira/pure/researchoutput/libraryofcongress/qh301
Subjects:
ID Code:
34792
Deposited By:
Deposited On:
13 Dec 2010 09:08
Refereed?:
Yes
Published?:
Published
Last Modified:
10 May 2020 02:14