HOU Dan-dan, WANG Yun-long, ZHANG Yi-qing, et al. Optimization of measles virus N protein's prokaryotic expression and purification[J]. Journal of Light Industry, 2013, 28(6): 32-34,47. doi: 10.3969/j.issn.2095-476X.2013.06.008
Citation:
HOU Dan-dan, WANG Yun-long, ZHANG Yi-qing, et al. Optimization of measles virus N protein's prokaryotic expression and purification[J]. Journal of Light Industry, 2013, 28(6): 32-34,47.
doi:
10.3969/j.issn.2095-476X.2013.06.008
Optimization of measles virus N protein's prokaryotic expression and purification
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College of Life Science, He'nan Normal University, Xinxiang 453007, China;
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College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China;
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He'nan Biotechnology Research Center, Zhengzhou 450001, China
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Corresponding author:
WANG Yun-long,
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Received Date:
2013-04-12
Available Online:
2013-11-15
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Abstract
In order to construct a recombinant expression plasmid which induced express purification measles virus(MV) N protein, the recombinant plamised of pET-32 a(+)/N amplified by PCR from MV N protein genes was inserted into expression vector pET-32 a(+), then it was transformed into E. coli BL21(DE3). The condition of time, temperature and concentration of IPTG were optimized. The results of SDSPAGE and Western blot tests showed that MV N protein molecular was 60 kD. The protein's purity was 90% after being purified by Ni-NTA and DEAE.
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References
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