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构建了抗人卵巢癌×抗人CD3双特异性单链抗体 (scBsAb) ,在大肠杆菌中得到表达。用稀释复性 ,缓慢透析复性和凝胶过滤层析复性三种方法对scBsAb表达形成的包涵体进行复性研究表明 ,凝胶过滤层析复性能有效抑制蛋白的聚集。ELISA检测显示 ,复性后的scBsAb具有较高活性 ,能与相应抗原特异结合。
Anti-human ovarian cancer × anti-human CD3 bispecific single chain antibody (scBsAb) was constructed and expressed in E. coli. The renaturation of inclusion bodies formed by scBsAb expression using three methods of dilution refolding, slow dialysis refolding and gel filtration chromatography renaturation showed that refolding by gel filtration chromatography could effectively inhibit protein aggregation. ELISA test showed that the refolded scBsAb has high activity and can specifically bind to the corresponding antigen.