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本文用FasL单抗NOK 1与CNBr Sepharose4B偶联 ,制备亲和层析柱 ,从表达FasL的HEpG2细胞膜蛋白抽提液中分离纯化FasL分子。实验证明用本法纯化的FasL其相对分子质量为 3 10 0 0～ 3 3 0 0 0 ,SDS PAGE呈现单一条带 ,Westernblot表明具有一定的抗原性 ,能诱导表达Fas的细胞发生凋亡 ,在一定浓度范围内呈现量 效关系 ,为进一步研究FasL分子的结构功能及制备抗体提供了实验材料。
In this paper, FasL monoclonal antibody NOK 1 was coupled with CNBr Sepharose 4B to prepare an affinity chromatography column, and the FasL molecules were isolated and purified from the membrane protein extract of HEpG2 cells expressing FasL. Experiments show that this method of purification of the relative molecular mass of the FasL relative molecular mass of 3 10 0 0 to 3 0 0 0, SDS PAGE showed a single band, Western blot showed a certain antigenicity can induce apoptosis of Fas-expressing cells in A dose-effect relationship exists within a certain concentration range, providing experimental materials for further study on the structural function of FasL molecules and preparation of antibodies.