Iber H, Sandhoff K
Institut für Organische Chemie und Biochemie der Universität Bonn, FRG.
FEBS Lett. 1989 Aug 28;254(1-2):124-8. doi: 10.1016/0014-5793(89)81022-1.
Competition experiments using GM1b, GD1a and GT1b as substrates, and as mutual inhibitors for ganglioside sialyltransferase activity in preparations of Golgi vesicles derived from rat liver, suggested that sialyl transfer to these three respective compounds, leading to gangliosides GD1C, GT1a and GQ1b, respectively, is catalyzed by one enzyme. These results are incorporated into a model for ganglioside biosynthesis and its regulation.
使用GM1b、GD1a和GT1b作为底物,并作为大鼠肝脏来源的高尔基体囊泡制剂中神经节苷脂唾液酸转移酶活性的相互抑制剂进行的竞争实验表明,分别导致神经节苷脂GD1C、GT1a和GQ1b的向这三种相应化合物的唾液酸转移是由一种酶催化的。这些结果被纳入神经节苷脂生物合成及其调控模型中。