【摘要】 将人工合成的寡核苷酸片段 ,通过PCR扩增得到死亡肽 (thanatin)基因 ,并将其克隆到表达载体pGEX 3X中 ,序列分析结果正确。经IPTG诱导 ,在大肠杆菌BL2 1中进行高效可溶性表达 ,表达量可达 2 0 %以上。融合蛋白通过GST亲和层析纯化 ,用肠激酶酶解表达产物 ,用SephadexG 2 5初步纯化得到具有抗菌活性的死亡肽。更多还原

【Abstract】 The thanatin gene was obtained and inserted into expression vector pGEX-3X by a DNA recombinant method which was checked by nucleotide sequencing. The fusion protein of GST-thanatin was produced by IPTG induction in Escherichia coli (BL21). The expression level was about 20%. The fusion protein was purified by GST affinity chromatography and digested by enterokinase. Partly purified with Sephadex G-25, the final product, thanatin exhibited antimicrobial activity.更多还原