Reinwald E, Greiser-Wilke I, Artama W, Risse H J, Mölling K
Institut für Veterinär-Biochemie, Freie Universität Berlin.
Eur J Biochem. 1987 Sep 15;167(3):525-32. doi: 10.1111/j.1432-1033.1987.tb13369.x.
Monoclonal antibodies were isolated from mice immunized with variant surface glycoprotein of Trypanosoma congolense. Five out of the six monoclonals were able to detect epitopes at the cell surface in an indirect immunofluorescence analysis. One antibody did not react. Using protein-A-containing bacterial adsorbent all monoclonal antibodies precipitate glycosylated as well as non-glycosylated variant surface glycoprotein. Carbohydrate chains therefore do not appear to be part of the immunodeterminant structure recognized by the various monoclonal antibodies. Interaction of the monoclonal antibodies with protein fragments obtained by partial proteolysis with V8 protease from Staphylococcus aureus or papain allows the classification of the antibodies into three groups with different epitope specificity.
从用刚果锥虫可变表面糖蛋白免疫的小鼠中分离出单克隆抗体。在间接免疫荧光分析中，六种单克隆抗体中有五种能够检测到细胞表面的表位。一种抗体没有反应。使用含蛋白A的细菌吸附剂，所有单克隆抗体均可沉淀糖基化和非糖基化的可变表面糖蛋白。因此，碳水化合物链似乎不是各种单克隆抗体识别的免疫决定结构的一部分。单克隆抗体与通过用来自金黄色葡萄球菌的V8蛋白酶或木瓜蛋白酶进行部分蛋白酶解获得的蛋白质片段的相互作用，可将抗体分为具有不同表位特异性的三组。
