中文摘要：

本研究首先构建了融合蛋白 TAT-p53-MTS 的原核表达质粒 pET-22b（＋）-TAT-p53-MTS,将表达纯化的融合蛋白与p53缺陷型人肺癌细胞NCI-H1299孵育,通过Western blot和免疫共沉淀（co-immunoprecipitation,co-IP）检测融合蛋白的细胞穿膜以及与 Bcl-2蛋白的相互作用,并通过流式细胞术检测融合蛋白对 NCI-H1299细胞的促凋亡作用。结果显示,融合TAT和MTS的p53重组蛋白具有更强的细胞穿膜及线粒体定位能力；并且,融合蛋白能够通过与Bcl-2蛋白的结合显著诱导NCI-H 1299细胞的凋亡。

英文摘要：

The plasmid for prokaryotic production of recombinant p5 3 fused with TAT and MTS （TAT-p5 3-MTS）was constructed.Purified recombinant protein was incubated with p5 3-deficient human lung cancer line NCl-H1299,and the cell lysate was subjected to co-immunoprecipitation and Western blot for testing the trans-membrane ability of the fusion protein,as well as the interaction between the fusion protein and Bcl-2.Additionally,flow cytometry was employed to detect fusion protein’s proapoptotic impact on NCl-H1299 cells.The results showed that TAT and MTS can improve both the trans-mem-brane ability and the mitochondrial targeting of the fusion protein.What’s more,the fusion protein ex-hibits ability to interact with Bcl-2,through which apoptosis is significantly induced.