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人胎盘催乳素在大肠杆菌中的表达
THE EXPRESSION OF HUMAN PLACENTAL LACTOGEN HORMONE IN E.COLI DH5α STRAIN
【摘要】 用 PCR方法扩增人胎盘催乳素 ( h PL) c DNA得到 597bp的片段 ,在其两端加上了合适的酶切位点及起始、终止密码子 ,将其与高效表达载体 p BV2 2 0重组连接 ,转入大肠杆菌 DH5α,得到稳定遗传的重组质粒转化子p BV-h PL.p BV-h PL菌株经热诱导后 ,有 2 2 k D的蛋白表达 ,表达量占菌体总蛋白的 1 2 .94 % ,h PL表达蛋白以包涵体形式存在 ,复性处理后 ,得到有生物活性的成熟蛋白
【Abstract】 By the method of PCR, human Placental Lactogen Hormone (hPL) cDNA 596bp was amplified and subcloned into a high efficient expression vector pBV220. The recombinant plasmid pBV hPL was obtained, which was very stable in E.coli DH5α. After induced with high temperature, a 22 kD protein was expressed, which accounted for 12.94% of the total cell protein. The hPL protein existed in the form of inactive inclusion body, by the way of renaturation, the active mature protein was obtained.
- 【文献出处】 南开大学学报(自然科学版) ,JOURNAL OF NANKAI UNIVERSITY , 编辑部邮箱 ,2000年03期
- 【分类号】Q786
- 【下载频次】39