A beta-galactoside alpha 1 leads to 2 fucosyltransferase has been solubilized from porcine submaxillary glands and purified 124,000-fold to homogeneity by repeated affinity chromatography on GDP-hexanolamine agarose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the purified enzyme revealed two electrophoretic species with apparent Mr = 60,000 and 55,000. The two enzyme species have not been completely resolved, but both appear to be active forms of the fucosyltransferase with approximately equal specific activities. Glycosidase digestion of the fucosylated products with the alpha 1 leads to 2-specific fucosidase from Clostridium perfringens and the alpha 1 leads to 3/alpha 1 leads to 4-specific fucosidase from almond emulsin indicates that the enzyme forms exclusively the Fuc alpha 1 leads to 2Gal linkage with a variety of acceptor substrates. A GDP-fucose hydrolase activity co-purifies with the fucosyltransferase. Identical rates of thermal inactivation and co-migration on gel electrophoresis under nondenaturing conditions suggest that the two activities are due to a single enzyme species.