Optimization of measles virus N protein′s prokaryotic expression and purification
HOU Dan-dan
WANG Yun-long
ZHANG Yi-qing
SUN Xin-cheng
LI Yu-lin
MI Hai
WANG Ji-chuang
CHENG Lei
Abstract：In order to construct a recombinant expression plasmid which induced express purification mea-sles 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 SDS-PAGE 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.
Keywords：measles virusN proteinprokaryotic expressionprotein purification
Publication Date：2013-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：4( 32-34,47 )