Lauder, R. M. and Huckerby, T. N. and Nieduszynski, I. A. and Plaas, A. H. (1998) Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage. The Biochemical journal, 330 (. pp. 753-757.
Full text not available from this repository.Abstract
Bovine articular cartilage fibromodulin has been isolated from animals aged 3 months to 8 years, and the attached keratan sulphate (KS) chains digested with keratanase II. The oligosaccharides generated have been reduced, examined by high-pH anion-exchange chromatography and their structures identified by comparison with standards. It has been shown that in fibromodulin from young articular cartilage, the KS chains do not possess either non-reducing terminal (alpha2-6)-linked N-acetylneuraminic acid or fucose (alpha1-3)-linked to sulphated N-acetylglucosamine residues. However, an age-related increase has been observed in the abundance of both (alpha2-6)-linked N-acetylneuraminic acid and (alpha1-3)-linked fucose, neither of which is found in KS isolated from non-articular cartilage, irrespective of the age of the source. Interestingly, the KS chain length remains constant as a function of age, which possibly relates to a role in collagen fibril assembly. In addition, no significant age-related changes were identified in levels of galactose sulphation.
| Item Type: | Article |
|---|---|
| Journal or Publication Title: | The Biochemical journal |
| Subjects: | R Medicine > R Medicine (General) |
| Departments: | Faculty of Health and Medicine > Biomedical & Life Sciences Faculty of Science and Technology > Lancaster Environment Centre |
| ID Code: | 34810 |
| Deposited By: | Dr Bob Lauder |
| Deposited On: | 09 Dec 2010 09:29 |
| Refereed?: | No |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 17:41 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/34810 |
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