Lund T, Bravo R, Johansen H R, Zeuthen J, Vuust J
FEBS Lett. 1986 Nov 24;208(2):369-72. doi: 10.1016/0014-5793(86)81051-1.
Rat immunoglobulin E (IgE) synthesized in Xenopus laevis oocytes, injected with rat plasmacytoma mRNA, was analysed by specific immunoprecipitation and SDS-polyacrylamide gel electrophoresis under reducing as well as non-reducing conditions. The results indicate that the oocytes will translate and correctly process the rat IgE heavy and light chains, resulting in secretion of a correctly assembled, normal immunoglobulin molecule. The normal, extensive glycosylation of the IgE heavy chain (e-chain) is faithfully carried out by the oocytes; therefore, this posttranslational modification is apparently of an unspecific nature, and does not depend upon a mechanism specific for plasma cells.
将大鼠浆细胞瘤mRNA注入非洲爪蟾卵母细胞中，使其合成大鼠免疫球蛋白E（IgE），然后在还原和非还原条件下通过特异性免疫沉淀和SDS-聚丙烯酰胺凝胶电泳对其进行分析。结果表明，卵母细胞能够翻译并正确加工大鼠IgE重链和轻链，从而分泌出正确组装的正常免疫球蛋白分子。卵母细胞忠实地完成了IgE重链（e链）正常且广泛的糖基化；因此，这种翻译后修饰显然是非特异性的，并不依赖于浆细胞特有的机制。
