Study of the Fucosyltransferase System in Intestinal Microsomes

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Abstract
Fucosyltransferase activity of rat small intestine microsomes is solubilized by 0.5% Triton X-100. The solubilized activity can be purified up to 8,300-fold using DEAEcellulose and affinity chromatography on GDP-Sepharose. At this step, chromatography on Sephadex Gl5 separates different specificities: N-acetylglucosaminide-a-(l,3)-fucosyltransferase acting on asialoserotransferrin, and galactoside-a-( 1,2)-fucosyltransferase acting on O-glycans of asialofetuin. The use of small saccharidic acceptors also indicates the presence of a N-acetylglucosaminide-α-( 1,4)-fucosyltransferase and of a very weak glucose-α-(l,3)- fucosyltransferase activity. These activities are tightly bound to concanavalin A-Sepharose, suggesting that they are supported by N-glycosylproteins.