Bierfreund U, Lemm T, Hoffmann A, Uhlhorn-Dierks G, Childs R A, Yuen C T, Feizi T, Sandhoff K
Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, Germany.
Neurochem Res. 1999 Feb;24(2):295-300. doi: 10.1023/a:1022526407855.
The interaction between glycosphingolipids and recombinant human GM2-activator was studied in a microwell binding assay. A-series gangliosides like GM3, GM2 and GM1 were strongly bound by the recombinant human GM2 activator. A weak binding was observed to GD1b and sulfatide, while neutral glycolipids were not bound. Optimal binding occurred at pH 4.2 and was inhibited by increasing concentrations of citrate buffer and NaCl. In contrast with these in vitro results the recombinant human GM2-activator is able to restore the degradation of GA2 in fibroblasts from patients with the AB variant of GM2 gangliosidosis in vivo.
在微孔板结合试验中研究了糖鞘脂与重组人GM2激活剂之间的相互作用。GM3、GM2和GM1等A系列神经节苷脂被重组人GM2激活剂强烈结合。观察到与GD1b和硫苷脂有弱结合，而中性糖脂未结合。最佳结合发生在pH 4.2，并且随着柠檬酸盐缓冲液和NaCl浓度的增加而受到抑制。与这些体外结果相反，重组人GM2激活剂能够在体内恢复GM2神经节苷脂病AB变异型患者成纤维细胞中GA2的降解。
