Construction of High Expression System of Human Plasminogen Kringle 5 （hPK-5） Protein in E.coliChinese Full Text
CHEN Xian-jiu, WANG Hui-zhen,YU Bao-feng, et al (Department of Biochemistry and Molecular Biology, Shanxi Medical University, Taiyuan 030001)
Abstract: Objective To construct a high expression system of human plasminogen kringle 5 （hPK-5） protein in E.coli and establish optimal conditions for high density fermentation.Methods Observe the growth of bacterial seeds of classes I and II, compare the expression levels of hPK-5 protein in 4 recombinant strains under the same conditions, select the optimal seeds and further optimize the conditions for fermentation, including the time for culture and induction, medium and pH value. Analyze the bands showed in SDS-PAGE by gel image-forming analysis system.Results JM109/pBV220/hPK-5 （JP5） was selected as the optimal recombinant strain for the expression of hPK-5 protein, and the optimal condition for expression was as follows: inoculate the optimal recombinant strain onto LB medium （pH7.4, with dissolving oxygen supplied well） and incubate at 30℃ for 3h, then induce at 42℃ for 6h. The expression level of JP5 protein under this condition reached about 38% of total somatic protein.Conclusion The study laid an experimental basis of preparing hPK-5 protein by high density fermentation.
- DOI：
10.13200/j.cjb.2004.04.15.chenxj.005
- Series：
- Subject：
- Classification Code：
R346
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