Structural studies of two populations of keratan sulphate chains from mature bovine articular cartilage |
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Authors: | David J Thornton Haydn G Morris Gordon H Cockin Thomas N Huckerby Ian A Nieduszynski |
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Institution: | (1) Division of Biological Sciences, Institute of Environmental and Biological Sciences, University of Lancaster, Bailrigg, LA1 4YQ Lancaster, U.K.;(2) Department of Chemistry, University of Lancaster, Bailrigg, LA1 4YA Lancaster, U.K.;(3) Present address: Department of Biochemistry, University of Manchester, Stopford Building, Oxford Road, M13 9PT Manchester, U.K. |
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Abstract: | Two discrete peptido-keratan sulphate fragments were isolatedvia chondroitinase ABC and trypsin digestion of a proteoglycan aggregate fraction prepared from bovine femoral head cartilage (six year old animals). The larger fragments (Kav=0.07, CL-6B) contained peptides substituted with several keratan sulphate (KS) chains from the KS-rich region of the proteoglycan and the smaller fragments (Kav=0.5, CL-6B) contained peptides with, perhaps, only one KS chain and the stubs of post-chondroitinase-treated chondroitin sulphate chains.The two peptido-KS samples and the KS chains derived from these by alkaline borohydride reduction were characterised by13C-NMR spectroscopy. The two populations of KS chains were also examined by chromatography (Sephadex G-75), and keratanase digestion followed by chromatography on Bio-Gel P-10. From the results it was concluded that the KS chains from the two major trypsin-derived peptido-KS fragments had similar sulphation levels, distributions of hydrodynamic sizes and susceptibilities to keratanase.Abbreviations KS
keratan sulphate
- A1
proteoglycan aggregate
- T
diphenyl carbamyl chloride (DPCC)-trypsintreated
- CB
chondroitinase ABC-treated
- C
chymotrypsin-treated
- P
papain-treated
- R
alkaline borohydride-reduced
- TSP
sodium 3-trimethylsilylpropionate |
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Keywords: | keratan sulphate NMR spectroscopy articular cartilage |
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