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)
