Helm R M, Conrad D H, Froese A
Int Arch Allergy Appl Immunol. 1979;58(1):90-8. doi: 10.1159/000232177.
Surface proteins and glycoproteins of RBL cells were labelled enzymatically with 125I and then solubilized with Nonidet P-40. Analysis by polyacrylamide-gel electrophoresis in SDS on 10% gel revealed 10 distinctive peaks ranging in molecular weights from 17,000 to 200,000 daltons. Mainly components of higher molecular weights were bound by lentil-lectin Sepharose and could be eluted with alpha-methyl mannoside. The receptor for IgE was clearly shown to bind to the lentil-lectin. A second cell surface component which previously had been shown to bind to IgE-Sepharose as well, was found to bind only slightly to lentil-lectin. Thus, it can be concluded that the receptor for IgE is a glycoprotein with mannose and/or N-acetylglucosamine in the carbohydrate moiety(s).
用125I对RBL细胞的表面蛋白和糖蛋白进行酶标记，然后用Nonidet P - 40使其溶解。在10%的凝胶上进行SDS聚丙烯酰胺凝胶电泳分析，结果显示有10个明显的峰，分子量范围为17,000至200,000道尔顿。较高分子量的主要成分与扁豆凝集素琼脂糖结合，并且可用α-甲基甘露糖苷洗脱。已清楚表明IgE受体与扁豆凝集素结合。还发现另一种先前已显示也能与IgE - 琼脂糖结合的细胞表面成分，它与扁豆凝集素的结合很微弱。因此，可以得出结论，IgE受体是一种在碳水化合物部分含有甘露糖和/或N - 乙酰葡糖胺的糖蛋白。
