One-Step Purification of an α(1-3)-L-Fucosyltransferase from Human Amniotic Fluid by Fetuin-Agarose Affinity Chromatography

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Abstract
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.