中文摘要：

目的获取小鼠CD36基因片段，并高效表达和纯化GST—CD36融合蛋白。方法设计合成CD36的基因功能片段，测序后。通过酶切克隆至表达载体pGEX-5X-2，构建重组表达载体，并导入E．coli BL21宿主菌中，异丙基硫代半乳糖苷（PTG）诱导表达重组的GST融合蛋白，亲和层析纯化表达产物，SDS—PAGE进行分析鉴定。结果获得小鼠CD36基因片段，测序结果与GenBank的基因序列一致，重组GST融合蛋白经SDS—PAGE分析，在相对分子量28．5kDa处，出现特异性蛋白条带，重组蛋白经GST亲和层析柱纯化后，得到了高纯度的融合蛋白。结论合成小鼠CD36基因片段，并在E．coli BL21中高效表达，亲和层析后获得高纯度GST—CD36融合蛋白。

英文摘要：

Objective To obtain mouse CD36 segments that express efficiendy in E.coli BL21 and purify the target proteins. Methods CD36 gene segments were designed and synthesized. After sequenced, the reconstructed expression vectors were constructed by enzyme digestion and cloning into expression vector pGEX-5X-2. Then the reconstructed vectors were transformed into E.coli BL21. Recombinant GST fusion proteins were expressed via the induction of IPTG and purified through GST affinity columns. Results The sequences of cloned mouse CD36 gene segments were identical with GenBank reported. A protein band of 28.5 kDa appeared on SDS-PAGE gel after the expressed GST fusion proteins were separated by SDS-PAGE. Then the expressed fusion proteins were purified to highpurity. Conclusion The mouse CD36 gene segments have been synthesized and efficiendy expressed in E.coli BL21 ,and the GST fused target proteins have been purified to high purity.