13C-NMR spectroscopy of keratan sulphates--assignments for five sialylated pentasaccharides derived from the non-reducing chain termini of bovine articular cartilage keratan sulphate by keratanase II digestion

Biomedical and Life Sciences

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https://doi.org/10.1046/j.1432-1327.1998.2510991.x
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Keywords

Acetylglucosaminidase, Animals, Carbohydrate Conformation, Carbohydrate Sequence, Carbon Isotopes, Cartilage, Articular, Cattle, Keratan Sulfate, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oligosaccharides

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13C-NMR spectroscopy of keratan sulphates--assignments for five sialylated pentasaccharides derived from the non-reducing chain termini of bovine articular cartilage keratan sulphate by keratanase II digestion. / Huckerby, T N; Brown, Gavin; Nieduszynski, I A.
In: European Journal of Biochemistry, Vol. 251, No. 3, 02.1998, p. 991-997.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{63037ac1124848a5b628f10bd90ac230,

title = "13C-NMR spectroscopy of keratan sulphates--assignments for five sialylated pentasaccharides derived from the non-reducing chain termini of bovine articular cartilage keratan sulphate by keratanase II digestion",

abstract = "Skeletal keratan sulphate has been fragmented using the enzyme keratanase II, and 13C chemical-shift data are reported for five reduced sialylated pentasaccharides that derived from the non-reducing chain terminal region. They have the structures: NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal6S(beta1-4)++ +GlcNAc6S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)Glc NAc6S-ol, and NeuAc(alpha2-3)Gal(6S)(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)++ +GlcNAc6S-ol, where GlcNAc6S-ol represents N-acetyl-glucosaminitol 6-O-sulphate and NeuAc represents N-acetylneuraminic acid. The use of these 13C-NMR spectroscopy data for the recognition of specific chain-capping structures within native keratan sulphates is discussed. In addition, examination of the data derived from the NeuAc(alpha2-6) capping structures strongly suggests that sulphation three residues away from the neuraminic acid cap has a profound effect upon the conformation of the capping region.",

keywords = "Acetylglucosaminidase, Animals, Carbohydrate Conformation, Carbohydrate Sequence, Carbon Isotopes, Cartilage, Articular, Cattle, Keratan Sulfate, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oligosaccharides",

author = "Huckerby, {T N} and Gavin Brown and Nieduszynski, {I A}",

year = "1998",

month = feb,

doi = "10.1046/j.1432-1327.1998.2510991.x",

language = "English",

volume = "251",

pages = "991--997",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell",

number = "3",

}

RIS

TY - JOUR

T1 - 13C-NMR spectroscopy of keratan sulphates--assignments for five sialylated pentasaccharides derived from the non-reducing chain termini of bovine articular cartilage keratan sulphate by keratanase II digestion

AU - Huckerby, T N

AU - Brown, Gavin

AU - Nieduszynski, I A

PY - 1998/2

Y1 - 1998/2

N2 - Skeletal keratan sulphate has been fragmented using the enzyme keratanase II, and 13C chemical-shift data are reported for five reduced sialylated pentasaccharides that derived from the non-reducing chain terminal region. They have the structures: NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal6S(beta1-4)++ +GlcNAc6S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)Glc NAc6S-ol, and NeuAc(alpha2-3)Gal(6S)(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)++ +GlcNAc6S-ol, where GlcNAc6S-ol represents N-acetyl-glucosaminitol 6-O-sulphate and NeuAc represents N-acetylneuraminic acid. The use of these 13C-NMR spectroscopy data for the recognition of specific chain-capping structures within native keratan sulphates is discussed. In addition, examination of the data derived from the NeuAc(alpha2-6) capping structures strongly suggests that sulphation three residues away from the neuraminic acid cap has a profound effect upon the conformation of the capping region.

AB - Skeletal keratan sulphate has been fragmented using the enzyme keratanase II, and 13C chemical-shift data are reported for five reduced sialylated pentasaccharides that derived from the non-reducing chain terminal region. They have the structures: NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(beta1-4)GlcNAc6 S-ol, NeuAc(alpha2-6)Gal(beta1-4)GlcNAc6S(beta1-3)Gal6S(beta1-4)++ +GlcNAc6S-ol, NeuAc(alpha2-3)Gal(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)Glc NAc6S-ol, and NeuAc(alpha2-3)Gal(6S)(beta1-4)GlcNAc6S(beta1-3)Gal(6S)(beta1-4)++ +GlcNAc6S-ol, where GlcNAc6S-ol represents N-acetyl-glucosaminitol 6-O-sulphate and NeuAc represents N-acetylneuraminic acid. The use of these 13C-NMR spectroscopy data for the recognition of specific chain-capping structures within native keratan sulphates is discussed. In addition, examination of the data derived from the NeuAc(alpha2-6) capping structures strongly suggests that sulphation three residues away from the neuraminic acid cap has a profound effect upon the conformation of the capping region.

KW - Acetylglucosaminidase

KW - Animals

KW - Carbohydrate Conformation

KW - Carbohydrate Sequence

KW - Carbon Isotopes

KW - Cartilage, Articular

KW - Cattle

KW - Keratan Sulfate

KW - Molecular Sequence Data

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Oligosaccharides

U2 - 10.1046/j.1432-1327.1998.2510991.x

DO - 10.1046/j.1432-1327.1998.2510991.x

M3 - Journal article

C2 - 9490077

VL - 251

SP - 991

EP - 997

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

IS - 3

ER -

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