中文摘要：

以pErl30a为载体构建的表达拟南芥热激因子AtHsfAla的大肠杆菌EcoliM15（pET30a／His6一AtHsfAla）为实验材料，以IPTG诱导6XHis融合蛋白的表达并经过Ni2＋柱分离纯化AtHsfAla，再通过SDS—PAGE鉴定表达蛋白和纯化蛋白．结果显示，AtHsfAla蛋白在在PET原核表达系统中能够有效表达，并能通过亲和层析获得纯化的AtHsfAla蛋白．研究结果为揭示拟南芥热激因子AtHsfAla的作用机理奠定基础．

英文摘要：

E coli M15 （ （pET30a His6-AtAtHsfAla） was used as experimental materials. Expression of AtHsfA1 a in Arabidopsis thaliana was induced with isopropyl-13-D-galactoside （IPTG）. AtHsfAla was purified by the Ni-NTA-Agarose affinity chromatography. AtHsfAla was analyzed by the SDS-PAGE eleetrophoresis. Heat shock factor HsfAla in Arabidopsis thaliana was expressed and purified. The result showed that experimental material was provided for isolating and identifying of heat shock elements （ HSE ） bound in vivo by heat shock factor HSF in Arabidopsis thaliana and founded the basis for the function mechanism of heat shock factor AtHsfAla.