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The structure of a major fucose-containing sugar sequence of rat brain glycoproteins was investigated. Glycopeptides obtained by proteolytic digestion of the lipid-free residue of whole rat brain were fractionated by affinity chromatography on Sepharose bound to concanavalin A and wheat-germ agglutinin. An N-glycosidic glycopeptide fraction corresponding to about 65% of the protein-bound fucose was obtained. Methylation analysis before and after treatment with α-fucosidase or mild acid demonstrated that a major proportion of fucose is linked to the C-3 of N-acetylglucosamine. Studies involving neuraminidase digestion, partial acid hydrolysis, chromium trioxide oxidation and uronic acid degradation revealed that the fucose-containing sugar sequence has the structure: The structure of the Gal(β1–4) Fuc(α1–3)GlcNAc sequence was also confirmed by gas-liquid chromatography and mass spectrometry after preparation of an oligosaccharide derivative by specific degradation with nitrous acid deamination. The sugar sequence, which has not previously been described in glycoproteins, is a sialosylated derivative of the so-called X antigen structure and it accounts for most of the fucose present in brain glycoproteins. The sugar sequence occurs mainly in membrane-bound glycoproteins, but is also found in the soluble fraction.
Krusius et al. (Wed,) studied this question.
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