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Characterisation of a nonreducing terminal fragment from bovine articular-cartilage keratan sulfates containing alpha(2-3)-linked sialic-acid and alpha(1-3)-linked fucose.

Research output: Contribution to Journal/MagazineJournal article

<mark>Journal publication date</mark>10/1996
<mark>Journal</mark>Biochemical Journal
Issue number1
Number of pages5
Pages (from-to)137-141
Publication StatusPublished
<mark>Original language</mark>English


Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6–8-year-old animals) and digested with keratanase II, an endo-b-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 a(2-3)-linked sialic acid and a(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-Lex structure [NeuAca2-3Galb1-4(Fuca1-3)GlcNAcb1-] was identified in this study.