中文摘要：

目的：探索大肠杆菌原核表达系统制备具有生物功能的抗菌肽的最佳诱导条件。方法：将富甘氨酸果蝇抗菌肽基因的核心片段构建表达载体pET32a＋中，经序列分析证实基因序列的正确性。在不同温度、不同时间和不同IPTG浓度进行诱导后，用15％SDS—PAGE检测融合蛋白的表达，发现有一条分子量约8kD的新增蛋白条带。结果：研究表明在37℃菌液OD值0．8时诱导7h蛋白表达量最高（IPTG0．7mmol/L，AMP100μg/ml，0．3％Glu）。结论：获得了抗菌肽表达的最佳诱导条件，为大量诱导产生该抗菌肽奠定了理论基础。

英文摘要：

Objective：To explore the expression optimal condition of a novel glycine- rich antibacterial peptide from Drosophila in Escher/ch/a co- li. Method： The core fragment encoding a novel glycine - rich antibacterial peptide gene was cloned into pET32a ＋ plasmid, After sequencing, the recombinant clone was transferred into competent ceils of E. coli BI2.1（DE3） and was induced by different IFI＇G under different temperature ,different time, different OD. By 15% SDS- PAGE detection, A new 8 kD was found. Result： The expression optimal condition was 37℃,OD 0.8,7 horns, IPTG 0.7mmol/L, LB media （AMP 100μg/ml, 0.3% Glu）. Conclusion： The expression optimal condition of antibacterial peptide was successfully obtained.