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. 1988 Jul 15:178:23-8.
doi: 10.1016/0008-6215(88)80099-5.

Biosynthesis of cancer-associated sialyl-X antigen by a (1----3)-alpha-L-fucosyltransferase of human amniotic fluid

F G Hanisch  1 , A Mitsakos, H Schroten, G Uhlenbruck
Affiliations

Biosynthesis of cancer-associated sialyl-X antigen by a (1----3)-alpha-L-fucosyltransferase of human amniotic fluid

F G Hanisch et al. Carbohydr Res. .

Abstract

Activity of a hitherto unknown (1----3)-alpha-L-fucosyltransferase that acts on IV3-alpha-NeuAc-nLcOseCer as acceptor substrate was demonstrated in human amniotic fluid. The 14C-labelled product IV3-alpha-NeuAc-III3-alpha-Fuc-nLcOseCer was detected autoradiographically after t.l.c. and identified after desialylation by immunostaining with monoclonal antibody Leu Ml. The enzyme is assumed also to catalyze the last step in the biosynthesis of sialyl-X antigen carried by mucins in human amniotic fluid.

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