中文摘要：

[目的]构建枯草芽孢杆菌硫氧还蛋白还原酶（thioredoxin reductase，TrxR）原核载体，表达、纯化TrxR重组蛋白，制备并鉴定多克隆抗体。[方法]通过分子克隆获得TrxR蛋白的表达菌株；利用镍离子亲和层析获得纯化的TDcR重组蛋白，免疫兔子制备TrxR蛋白多克隆抗体；采用ELISA法测定抗体效价；WesternBlot检测抗血清的特异性。[结果]TrxR重组载体双酶切结果与DNA测序鉴定结果一致，蛋白表达纯化条带大小与预测一致。ELISA法测定抗血清效价为7×10^4，Western Blot证实抗血清有较高的特异性。[结论]成功克隆、表达与纯化TrxR重组蛋白，制备并鉴定兔子多克隆抗体，为TrxR的生物学功能研究奠定基础。

英文摘要：

[ Objective ] To construct prokaryotic expression vector of Bacillus subtilis thioredoxin reduetase （TrxR）, expressed and purified TrxR, prepared and identified the polyclonal antibodies of rabbit anti - TrxR. [ Methods ] The TrxR expression strain was obtained by molecular method; The recombinant protein TrxR was purified by the way of nickel ion affinity chromatography,and immunized rabbit to prepare the polyclonal antibody;The antibody titer and specificity were detected by ELISA and Western Blotting, respectively. [ Results] TrxR recombinant vector had been digested and sequenced to confirm the correct construction. TrxR expression and purification of strip size agreed with the prediction. The TrxR antibody titer was 7 × 10^4 by ELISA,and Western Blot proved that the antiserum had better specificity. [ Conclusion] Succession of cloning of TrxR expression vector, expression and purification acquired TrxR, prepared and identified the rabbit polyclonal antibodies of TrxR. These work laid the foundation work for the biology function research of TrxR.