A sub-population of keratan sulphates derived from bovine articular cartilage is capped with alpha(2-6)-linked N-acetylneuraminic acid residues. Affinity chromatography using immobilized Sambucus nigra lectin and characterization using 1H n.m.r. spectroscopy

Biomedical and Life Sciences

Keywords

Animals, Carbohydrate Conformation, Carbohydrate Sequence, Cartilage, Articular, Cattle, Chromatography, Affinity, Keratan Sulfate, Lectins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, N-Acetylneuraminic Acid, Plant Lectins, Ribosome Inactivating Proteins, Sialic Acids

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A sub-population of keratan sulphates derived from bovine articular cartilage is capped with alpha(2-6)-linked N-acetylneuraminic acid residues. Affinity chromatography using immobilized Sambucus nigra lectin and characterization using 1H n.m.r. spectroscopy. / Tai, G H; Morris, H G; Brown, G M et al.
In: Biochemical Journal, Vol. 286 , No. 1, 1992, p. 231-234.

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

Bibtex

@article{7c2d91e8d61247cda1f71d38bcda571e,

title = "A sub-population of keratan sulphates derived from bovine articular cartilage is capped with alpha(2-6)-linked N-acetylneuraminic acid residues. Affinity chromatography using immobilized Sambucus nigra lectin and characterization using 1H n.m.r. spectroscopy",

abstract = "Alkaline borohydride-reduced keratan sulphate (KS) chains derived from bovine femoral head cartilage were fractionated by lectin affinity chromatography with Sambucus nigra agglutinin (SNA) into binding and non-binding populations. Analysis of the SNA-binding and non-binding KS chains using 600 MHz 1H n.m.r. spectroscopy showed that the former population contained alpha(2-6)-N-acetylneuraminic acid residues and the latter contained primarily alpha(2-3)-N-acetylneuraminic acid residues as chain terminators. Both populations contained a similar proportion of alpha(2-3)-N-acetylneuraminic acid residues within their protein-linkage regions, and similar sulphation and fucosylation levels. Analysis of these two fractions by gel-permeation chromatography (g.p.c.) on a TSK-30 XL column showed them to have the same size distributions. It was concluded from the n.m.r. spectra and g.p.c. data that the populations differed primarily in the mode of linkage of the chain-terminating sialic acids.",

keywords = "Animals, Carbohydrate Conformation, Carbohydrate Sequence, Cartilage, Articular, Cattle, Chromatography, Affinity, Keratan Sulfate, Lectins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, N-Acetylneuraminic Acid, Plant Lectins, Ribosome Inactivating Proteins, Sialic Acids",

author = "Tai, {G H} and Morris, {H G} and Brown, {G M} and Huckerby, {T N} and Nieduszynski, {I A}",

year = "1992",

language = "English",

volume = "286 ",

pages = "231--234",

journal = "Biochemical Journal",

issn = "1470-8728",

publisher = "Portland Press Ltd.",

number = "1",

}

RIS

TY - JOUR

T1 - A sub-population of keratan sulphates derived from bovine articular cartilage is capped with alpha(2-6)-linked N-acetylneuraminic acid residues. Affinity chromatography using immobilized Sambucus nigra lectin and characterization using 1H n.m.r. spectroscopy

AU - Tai, G H

AU - Morris, H G

AU - Brown, G M

AU - Huckerby, T N

AU - Nieduszynski, I A

PY - 1992

Y1 - 1992

N2 - Alkaline borohydride-reduced keratan sulphate (KS) chains derived from bovine femoral head cartilage were fractionated by lectin affinity chromatography with Sambucus nigra agglutinin (SNA) into binding and non-binding populations. Analysis of the SNA-binding and non-binding KS chains using 600 MHz 1H n.m.r. spectroscopy showed that the former population contained alpha(2-6)-N-acetylneuraminic acid residues and the latter contained primarily alpha(2-3)-N-acetylneuraminic acid residues as chain terminators. Both populations contained a similar proportion of alpha(2-3)-N-acetylneuraminic acid residues within their protein-linkage regions, and similar sulphation and fucosylation levels. Analysis of these two fractions by gel-permeation chromatography (g.p.c.) on a TSK-30 XL column showed them to have the same size distributions. It was concluded from the n.m.r. spectra and g.p.c. data that the populations differed primarily in the mode of linkage of the chain-terminating sialic acids.

AB - Alkaline borohydride-reduced keratan sulphate (KS) chains derived from bovine femoral head cartilage were fractionated by lectin affinity chromatography with Sambucus nigra agglutinin (SNA) into binding and non-binding populations. Analysis of the SNA-binding and non-binding KS chains using 600 MHz 1H n.m.r. spectroscopy showed that the former population contained alpha(2-6)-N-acetylneuraminic acid residues and the latter contained primarily alpha(2-3)-N-acetylneuraminic acid residues as chain terminators. Both populations contained a similar proportion of alpha(2-3)-N-acetylneuraminic acid residues within their protein-linkage regions, and similar sulphation and fucosylation levels. Analysis of these two fractions by gel-permeation chromatography (g.p.c.) on a TSK-30 XL column showed them to have the same size distributions. It was concluded from the n.m.r. spectra and g.p.c. data that the populations differed primarily in the mode of linkage of the chain-terminating sialic acids.

KW - Animals

KW - Carbohydrate Conformation

KW - Carbohydrate Sequence

KW - Cartilage, Articular

KW - Cattle

KW - Chromatography, Affinity

KW - Keratan Sulfate

KW - Lectins

KW - Magnetic Resonance Spectroscopy

KW - Molecular Sequence Data

KW - N-Acetylneuraminic Acid

KW - Plant Lectins

KW - Ribosome Inactivating Proteins

KW - Sialic Acids

M3 - Journal article

C2 - 1520274

VL - 286

SP - 231

EP - 234

JO - Biochemical Journal

JF - Biochemical Journal

SN - 1470-8728

IS - 1

ER -

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