Skeletal keratan sulphate chains isolated from bovine intervertebral disc may terminate in alpha(2----6)-linked N-acetylneuraminic acid.
TLDR
The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha( 2----3) to an unsulphated galactose.Abstract:
Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (2-year-old animals) after digestion with chondroitin ABC lyase followed by digestion with diphenylcarbamoyl chloride-treated trypsin of A1D1 proteoglycans and gel-permeation chromatography on Sepharose CL-6B. The peptido-keratan sulphate fragments were subjected to alkaline borohydride reduction. The reduced chains were treated with keratanase in the presence of the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, and the digest was subjected to alkaline borohydride reduction. This produced oligosaccharides with galactitol at their reducing ends. This reduced digest was chromatographed on a Nucleosil 5 SB anion-exchange column and individual oligosaccharides were isolated. One of these was shown by 600 MHz 1H-n.m.r. spectroscopy to have the following structure: NeuAc alpha 2-6Gal beta 1-4GlcNAc(6-SO4)beta 1-3Gal-ol The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha(2----3) to an unsulphated galactose.read more
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Journal ArticleDOI
Keratan sulfate, a complex glycosaminoglycan with unique functional capability.
Bruce Caterson,James Melrose +1 more
TL;DR: Emerging evidence also suggest functional roles for the poly-N-acetyllactosamine regions of KS requiring further investigation, and further research is warranted to better understand the complexities of KS.
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High-performance liquid chromatographic analysis of glycosaminoglycan-derived oligosaccharides.
TL;DR: High-performance liquid chromatography of glycosaminoglycan (GAG)-derived oligosaccharides has been employed for the structural analysis and measurement of hyaluronan, chondroitin sulphate, dermatan sulphates, keratan sulphate and heparan sulphate.
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Structure of the O-linked carbohydrate chains of porcine zona pellucida glycoproteins
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TL;DR: Analysis of the endo-beta-galactosidase digests of pools of N- and O-glycans indicated that the two types of oligosaccharides contain qualitatively similar poly(N-acetyllactosamine) chains.
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Keratan sulfate disaccharide composition determined by FACE analysis of keratanase II and endo-β-galactosidase digestion products
TL;DR: The data illustrate that the FACE procedure represents an improved approach for accurate compositional microanalyses of corneal and skeletal keratan sulfates, especially applicable to experimentation involving small amounts of this glycosaminoglycan.
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Multiple non-reducing chain termini isolated from bovine corneal keratan sulfates.
TL;DR: Examination of the relative proportions of the capping to the repeat structures and knowledge of the average molecular size suggests that the sum of these non-reducing termini represents the caps of two antennae.