中文摘要：

目的构建GST．LM01融合蛋白表达载体，并在原核细胞大肠埃希菌（E．coli）中诱导表达。方法以人胎脑文库为模板，用PCR方法法扩增出LM01基因全长及各个截短突变体，通过BamHI和EcoRI酶切位点分别将其定向插入pGEX-5X-2载体中，构建原核表达质粒pGEX-5x-2-LM01及其截短突变体，通过酶切电泳鉴定和DNA序列测定正确后，转入E．coliBL21中，经异丙基硫代B—D半乳糖苷诱导表达，SDS—PAGE和Westernblot鉴定。结果酶切电泳及测序结果证明，成功构建了原核表达质粒pGEX-5x-2-LM01及其截短突变体，并用Westernblot方法证实了GST—LM01全长及各个截短突变体融合蛋白的表达。结论成功构建了LM01全长及其截短突变体原核表达载体，并证实了其在原核细胞大肠埃希菌中的表达，为LM01结构与功能的研究提供了前提基础。

英文摘要：

Objective To construct GST-LMO1 fusion protein expression vector and induce its expression in Escherichia coli （E.coli）. Methods The coding sequence of LM01 and its deletion fragrnents were amplified from the human fetal brain as the template by PCR and inserted into pGEX-5X-2 by BamH I and EcoR I . The positive recombinants were identified by restriction endonuclease digestion and DNA sequencing. Then they were transformed into E.coli BL21 ,induced by IPTG and identified by SDS -PAGE and Western blot. Results The prokaryotic expression plasmid pGEX-5X-2-LMO1 and its deletion mutants were successfully constructed and confirmed by enzyme digestion and sequencing. The GST-LMO1 fusion proteins were expressed and confu＇med by Western blot. Conclusion The prokaryotic expression plasmid of LMO1 and its deletion mutants were srtccesshtlly constructed and the expression of fusion proteins in Eseherichia eoli was confirmed. This study provides the basis for the htrther research on the structure and function of LMO1.