Hanisch F G, Mitsakos A, Schroten H, Uhlenbruck G
Abteilung für Immunbiologie, 1. Medizinische Universitätsklinik, Köln, Federal Republik of Germany.
Carbohydr Res. 1988 Jul 15;178:23-8. doi: 10.1016/0008-6215(88)80099-5.
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.
在人羊水中证实了一种迄今未知的(1→3)-α-L-岩藻糖基转移酶的活性,该酶作用于IV3-α-NeuAc-nLcOseCer作为受体底物。经薄层层析后,通过放射自显影检测到14C标记的产物IV3-α-NeuAc-III3-α-Fuc-nLcOseCer,并在去唾液酸化后用单克隆抗体Leu M1免疫染色进行鉴定。据推测,该酶还催化人羊水中粘蛋白所携带的唾液酸化X抗原生物合成的最后一步。