摘要
本文对E.coliHB101菌株的外源基因表达产物"人γ-干扰素/人β-肿瘤坏死因子重组双功能杂交蛋白"(HuIFN-γ/HuTNF-β简称γTNFβ)进行了分离和初步纯化,并将产物作了抗病毒和细胞毒活性检测。结果表明,此初步纯化的γTNFβ的细胞毒活性为1.4×106u/mg·p;抗病毒活性为1.7×106u/mg·P。这一方法的建立,为进一步分离纯化γTNFβ打下了基础。
A recombinant hybrid protein──human interferon γ/tumor necrosis factor β(Hu IFNγ / TNFβ, γTNFβ) expressed by the extra fusion gene in E. coli HB 101 was identified and purified by means of micropore glass absorbed chromatography(MPG). It possesses dual functional activities of anti-virus and cytotoxin which are 1 .4 × 106u/mg protein and 1.7×106 u / mg protein respectively. This method has laid a foundation for the further study of γTNFβ's separation and purity function.
关键词
干扰素
肿瘤坏死因子
杂交蛋白
interferon(IFN)
tumor necrosis factor(TNF)
hybrid protein
micro-pore glass(MPG)