Bock E, Richter-Landsberg C, Faissner A, Schachner M
EMBO J. 1985 Nov;4(11):2765-8. doi: 10.1002/j.1460-2075.1985.tb04001.x.
The nerve growth factor-inducible large external (NILE) glycoprotein and the neural cell adhesion molecule L1 were shown to be immunochemically identical. Immunoprecipitation with L1 and NILE antibodies of [3H]fucose-labeled material from culture supernatants and detergent extracts of NGF-treated rat PC12 pheochromocytoma cells yielded comigrating bands by SDS-PAGE. NILE antibodies reacted with immunopurified L1 antigen, but not with N-CAM and other L2 epitope-bearing glycoproteins from adult mouse brain. Finally, by sequential immunoprecipitation from detergent extracts of [35S]methionine-labeled early post-natal cerebellar cell cultures or [3H]fucose-labeled NGF-treated PC12 cells, all immunoreactivity for NILE antibody could be removed by pre-clearing with L1 antibody and vice versa.
神经生长因子诱导的大外部(NILE)糖蛋白与神经细胞黏附分子L1在免疫化学上被证明是相同的。用L1和NILE抗体对来自经神经生长因子(NGF)处理的大鼠嗜铬细胞瘤PC12细胞的培养上清液和去污剂提取物中的[³H]岩藻糖标记物质进行免疫沉淀,通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)产生了共迁移条带。NILE抗体与免疫纯化的L1抗原发生反应,但不与成年小鼠脑内的神经细胞黏附分子(N-CAM)和其他带有L2表位的糖蛋白发生反应。最后,通过对[³⁵S]甲硫氨酸标记的出生后早期小脑细胞培养物的去污剂提取物或[³H]岩藻糖标记的经NGF处理的PC12细胞进行连续免疫沉淀,用L1抗体预清除可去除所有对NILE抗体的免疫反应性,反之亦然。