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

Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6–8-year-old animals) and digested with keratanase II, an endo-β-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 α(2-3)-linked sialic acid and α(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^x structure [NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-] was identified in this study.