One-step purification of an alpha(1-3)-L-fucosyltransferase from human amniotic fluid by fetuin-agarose affinity chromatography.

A soluble alpha(1-3)-L-fucosyltransferase, which accepts carbohydrates of the general structure NeuAc alpha(2-3)Gal beta(1-4)GlcNAc beta-R as substrates and which is involved in the biosynthesis of the tumor-associated sialyl-LeX determinant, was purified about 125-fold from human amniotic fluid by a one-step affinity chromatography on fetuin-agarose. Upon SDS gel electrophoresis, the purified enzyme revealed a protein band with a relative molecular mass (Mr) of about 62,000. The enzyme acted equally well on sialoglycoproteins and their desialylated derivatives.