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Characterization of oligosaccharides from the non‐reducing termini of keratan sulphate chains
Author(s) -
Huckerby Thomas N.,
Dickenson John M.,
Nieduszynski Ian A.
Publication year - 1992
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260301322
Subject(s) - chemistry , oligosaccharide , glycoside hydrolase , biochemistry , macromolecule , keratan sulfate , neuraminidase , stereochemistry , extracellular matrix , enzyme , proteoglycan
Abstract Keratan sulphate (KS) chains prepared from both bovine tracheal rings and bovine femoral head cartilage were digested with the enzyme keratanase from Pseudomonas species and non‐reducing terminal oligosaccharides were fractionated and purified using high‐performance ion‐exchange chromatography. Two oligosaccharides were fully characterized using one‐ and two‐dimensional NMR spectroscopic methods. An oligosaccharide derived from bovine tracheal ring KS chains was shown to have the structure NeuAcα 2–3 Galβ 1–4 GlcNAc(6‐SO 4 )β 1–3 Gal(6‐SO 4 )β 1–4 GlcNAc(6‐SO 4 )β 1–3 Gal‐ol (1). An oligosaccharide derived from bovine articular cartilage after treatment with a keratanase preparation containing neuraminidase activity was shown to have the structure Galβ 1–4 GlcNAc(6‐SO 4 )β 1–3 Gal(6‐SO 4 )β 1–4 GlcNAc(6‐SO 4 )β 1–3 Gal‐ol (2). These non‐reducing terminal structures are KS chain caps or terminators which, because of their accessibility, are likely to be involved in interactions with other macromolecules of the extracellular matrix.