Substrate Specificity of Cerebral GDP‐fucose: Glycoprotein Fucosyltransferase

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Abstract
Solubilized sheep brain fucosyltransferase was shown to transfer fucose from GDP-fucose onto glycoprotein and glycopeptide acceptors, e.g., asialofetuin, asialotransferrin, their glycopeptides and glycopeptides from ovalbumin, but not onto monosaccharides and disaccharides, e.g., galactose, N-acetylglucosamine and lactose. Competition studies between asialofetuin and glycopeptide V from ovalbumin provided evidence that both substrates compete for a common enzyme active site. Endo-.beta.-N-glucosaminidase D digestion of fucosylated and acetylated glycopeptide V showed that fucose is not linked to asparagine-linked N-acetylglucosamine. Hydrazinolysis and nitrous acid deamination performed on asialofetuin and glycopeptide V proved that fucose is not linked to external galactose or N-acetylglucosamine. It is assumed that fucose is linked to the oligomannochitobiosyl core of the glycan, probably to the second N-acetylglucosamine.

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