利用ＤＮＡ重组技术，在构建人γ干扰素突变体（ｈＩＦＮγ１３４Ｘ１３）表达质粒，取得高效表达的基础上，再将人β肿瘤坏死因子（ｈＴＮＦβ１４３，Ｎ端缺失２３ａａ）的ＤＮＡ片段亚克隆到该质粒外源编码序列的３′端，构建成人γ干扰素／β肿瘤坏死因子融合蛋白（ｈγＴＮＦβ）的重组基因表达质粒，转化大肠杆菌ＢＬ２１（ＤＥ３）。含有ｈγＴＮＦβ重组基因的阳性菌经温度（４２℃）诱导，在λＰＲＰＬ启动子的控制下，高效表达了ｈγＴＮＦβ。ＳＤＳＰＡＧＥ结果显示，在理论分子量３０ｋＤ处出现特异的目的蛋白表达带，表达量约占全菌蛋白的１８％。表达产物主要以不溶性的包涵体（ＩＢｓ）形式存在，通过分离纯化ＩＢｓ产物及复性处理，表达产物的抗病毒比活性与细胞毒比活性分别达到５０～５８×１０７ｕ／ｍｇｐ和４２～４９×１０７ｕ／ｍｇｐ。 Based on the recombinant DNA technology, we constructed the recombinant plasmid of human interferon gamma (hIFNγ134X13) and got high expression. Then, the DNA fragment of human βTumor necrosis factor (hTNFβ143, N-terminal deletion: 23aa) Was subcloned into the 3 ’end of the exogenous coding sequence of the plasmid to construct the recombinant gene expression plasmid of human γ interferon / β tumor necrosis factor fusion protein (hγTNF β) and transformed into E. coli BL21 (DE3). Positive bacteria containing hγTNFβ recombinant gene were induced by temperature (42 ℃), under the control of λPRPL promoter, hγTNFβ was highly expressed. SDS-PAGE showed that at the theoretical molecular weight of 30kD at a specific target protein expression zone, the expression of about 18% of the total bacterial protein. The products of expression mainly existed as insoluble inclusion bodies (IBs). The anti-virus specific activity and cytotoxic activity of the expressed products were 50 ~ 58 × 107u / mgp and 4  2 ~ 4  9 × 107u / mgp.