Fucosyltransferase was purified from human parotid saliva by affinity chromatography on GDP-hexanolamine Sepharose, followed by chromatofocusing on PBE 94 exchanger gel. The purified enzyme had the N-acetyglucosaminide alpha 1----4, the N-acetylglucosaminide alpha 1----3, and the glucoside alpha 1----3 fucosyltransferase activities. The molecular weight of the purified enzyme was estimated to be approximately 20,000. These enzyme activities showed identical pH and divalent metal ion dependencies and identical rates of inactivation upon being heated. The paper chromatographic analysis of the fucosylated products by the purified enzyme and the susceptibility of these products to linkage-specific fucosidase digestion indicated that the transferase formed the Fuc alpha 1----4GlcNAc, Fuc alpha 1----3GlcNAc, and Fuc alpha 1----3Glc linkages.