Biosynthesis of cancer-associated sialyl-X antigen by a (1----3)-alpha-L-fucosyltransferase of human amniotic fluid.
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.
D000653:Amniotic Fluid / Q000201:enzymology*; D002236:Carbohydrate Conformation; D002855:Chromatography, Thin Layer; D005647:Fucosyltransferases / Q000378:metabolism*; D006017:Glycolipids / Q000096:biosynthesis*; D006602:Hexosyltransferases / Q000378:metabolism*; D006801:Humans; D016256:Lewis X Antigen; D013997:Time Factors
D006017:Glycolipids; D016256:Lewis X Antigen; D005647:Fucosyltransferases; D006602:Hexosyltransferases; C031692:galactoside 3-fucosyltransferase