Abstract:
:The small keratan sulphate proteoglycan, fibromodulin, has been isolated from pooled human articular cartilage. The main chain repeat region and the chain caps from the attached N-linked keratan sulphate chains have been fragmented by keratanase II digestion, and the oligosaccharides generated have been reduced and isolated. Their structures and abundance have been determined by high pH anion-exchange chromatography. These regions of the keratan sulphate from human articular cartilage fibromodulin have been found to have the following general structure: [structure: see text]. Significantly, both alpha(2-6)- and alpha(2-3)-linked N-acetyl-neuraminic acid have been found in the capping oligosaccharides. Fucose, which is alpha(1-3)-linked as a branch to N-acetylglucosamine, has also been found along the length of the repeat region and in the capping region. The chains, which have been found to be very highly sulphated, are short; the length of the repeat region and chain caps is ca. nine disaccharides. These data demonstrate that the structure of the N-linked keratan sulphate chains of human articular cartilage fibromodulin is similar, in general, to articular cartilage derived O-linked keratan sulphate chains. Further, the general structure of the keratan sulphate chains attached to human articular cartilage fibromodulin has been found to be generally similar to that of both bovine and equine articular cartilage fibromodulin.
journal_name
Glycoconj Jjournal_title
Glycoconjugate journalauthors
Lauder RM,Huckerby TN,Nieduszynski IAdoi
10.1023/a:1018552913584subject
Has Abstractpub_date
1997-08-01 00:00:00pages
651-60issue
5eissn
0282-0080issn
1573-4986journal_volume
14pub_type
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journal_title:Glycoconjugate journal
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pub_type: 杂志文章
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journal_title:Glycoconjugate journal
pub_type: 杂志文章
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更新日期:1996-06-01 00:00:00
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journal_title:Glycoconjugate journal
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journal_title:Glycoconjugate journal
pub_type: 杂志文章
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更新日期:1991-02-01 00:00:00
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journal_title:Glycoconjugate journal
pub_type: 杂志文章
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更新日期:1997-01-01 00:00:00