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人胰岛素原在基因工程菌中的高效表达
引用本文:李红霞,余蓉,李晓红. 人胰岛素原在基因工程菌中的高效表达[J]. 华西药学杂志, 2005, 20(1): 14-17
作者姓名:李红霞  余蓉  李晓红
作者单位:四川大学华西药学院,四川,成都,610041;四川大学华西药学院,四川,成都,610041;四川大学华西药学院,四川,成都,610041
摘    要:目的 构建RRhPI-pQE4. 0E .coliM15表达系统 ,以高效表达 (His) 6 -Arg -Arg -人胰岛素原。方法 正交法优化发酵条件 ,通过湿菌体收率、包涵体收率及发酵液A60. 0 的测定对优化结果进行评估 ,并进一步分析发酵过程中主要因素对高密度发酵和高效表达的影响。结果 发酵条件优化后 ,每升发酵培养基可得湿菌体约 4 3g ,包涵体约 14g(湿重 )。结论 优化发酵条件可使湿菌体及包涵体的收率提高。

关 键 词:人胰岛素原  大肠杆菌(E.coli)  高效表达  (His)6-Arg-Arg-人胰岛素原
文章编号:1006-0103(2005)01-0014-04
修稿时间:2004-07-01

High expression of human proinsulin in Escherichia coli
LI Hong-xia,YU Rong ,LI Xiao-hong. High expression of human proinsulin in Escherichia coli[J]. West China Journal of Pharmaceutical Sciences, 2005, 20(1): 14-17
Authors:LI Hong-xia  YU Rong   LI Xiao-hong
Affiliation:LI Hong-xia,YU Rong *,LI Xiao-hong
Abstract:OBJECTIVE To express (His)6-Arg-Arg-human proinsulin by high density fermentation culture of RRhPI-pQE40 E.coli M15. METHODS The recombinant plasmid (His)6-Arg-Arg-human proinsulin (RRhPI)/pQE-40 was constructed successfully and was transformed into E.coli. The processs was optimized by orthogonal design. RESULTS High expression level of the gene product, which accumulated in inclusion bodies was obtained. 43 g wet E.coli cells and 14 g inclusion body were harvested from 1 L culture medium. CONCLUSION This study enhance the expression level of human proinsulin.
Keywords:Human proinsulin  Escherichia coli  High expression  (His)6-Arg-Arg-human proinsulin
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