Purification and Some Properties of Fucosyltransferase in Human Parotid Saliva

Abstract

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-acetylglucosaminide α1→4, the N-acetylglucosaminide α1→3, and the glucoside α1→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 α1→4GlcNAc, Fuc α1→3GlcNAc, and Fuc α1→3Glc linkages.