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Characterization of a non-reducing terminal fragment from bovine articular cartilage keratan sulphates containing alpha(2-3)-linked sialic acid and alpha(1-3)-linked fucose. A sulphated variant of the VIM-2 epitope.

ABSTRACT: Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6-8-year-old animals) and digested with keratanase II, an endo- beta-N-acetylglucosaminidase. The resulting oligosaccharides were borohydride-reduced and fractionated on a strong anion-exchange column. 1H-NMR spectroscopic analysis of the products revealed one containing both alpha(2-3)-linked sialic acid and alpha(1-3)-linked fucose which was shown to have the structure (I) shown. This structure is a sulphated variant of the VIM-2 epitope (CD65), a putative ligand of E-selectin. No oligosaccharide containing the sialyl-Le(+) structure [NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-] was identified in this study. [equation: see text]

SUBMITTER: Brown GM 

PROVIDER: S-EPMC1217746 | biostudies-literature | 1996 Oct

REPOSITORIES: biostudies-literature

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Characterization of a non-reducing terminal fragment from bovine articular cartilage keratan sulphates containing alpha(2-3)-linked sialic acid and alpha(1-3)-linked fucose. A sulphated variant of the VIM-2 epitope.

Brown G M GM   Huckerby T N TN   Abram B L BL   Nieduszynski I A IA  

The Biochemical journal 19961001

Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6-8-year-old animals) and digested with keratanase II, an endo- beta-N-acetylglucosaminidase. The resulting oligosaccharides were borohydride-reduced and fractionated on a strong anion-exchange column. 1H-NMR spectroscopic analysis of the products revealed one containing both alpha(2-3)-linked sialic acid and alpha(1-3)-linked fucose which was shown to have the structure (I) shown. This structure  ...[more]

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