Baltz T, Baltz D, Pautrizel R
Ann Immunol (Paris). 1976 Sep-Oct;127(5):761-74.
Binding of concanavalin A by different clones of Trypanosoma equiperdum was checked by its ability to agglutinate living trypanosomes. The clones differ by their agglutinability, showing differences in the distribution of the binding sites. However, the property of concanavalin A to form precipitates with the crude antigen preparations of all the clones studied, allowed to isolate by affinity chromatography the glycoprotein fraction responsible for the antigenic variation and to enter upon its physicochemical study.
通过刀豆球蛋白A凝集活锥虫的能力,检测了不同马媾疫锥虫克隆与刀豆球蛋白A的结合情况。这些克隆在凝集性方面存在差异,表明结合位点的分布有所不同。然而,刀豆球蛋白A与所有研究克隆的粗抗原制剂形成沉淀的特性,使得能够通过亲和层析分离出负责抗原变异的糖蛋白组分,并对其进行物理化学研究。