[Cloning and expression of superoxide dismutase gene from Deinococcus radiodurans in E. coli].
OBJECTIVE
To construct expressing recombinant of Mn-SOD of Deinococcus radiodurans and express the target protein in E. coli BL21(DE3).


METHODS
SOD gene was amplified by PCR from genomic DNA of Deinococcus radiodurans and inserted into expression plasmid pET-30a(+) to create the recombinant pET-SOD. After being analyzed by the restriction endonuclease, the plasmid was transformed into E. coli BL21(DE3), and the recombinant protein was expressed after induction by the isopropyl-beta-D-thiogalactopyranoside (IPTG) and was analyzed with SDS-PAGE.


RESULTS
The recombinant plasmid pET-SOD was obtained, and the recombinant protein was highly expressed in E. coli BL21(DE3). The activity of recombinant superoxide dismutase was 51,800 U per gram of wet bacteria.


CONCLUSIONS
This study has provided a foundation for further studies and applications of the recombinant Mn-SOD.
Meng
Ling
L
Department of Medical Technology, West China School of Public Health, Sichuan University, Chengdu 610041, China.
Xu
Xin
X
Wang
Dong-li
DL
Zhan
Li
L
Pei
Xiao-fang
XF
D003001:Cloning, Molecular; D034301:Deinococcus / Q000201:enzymology / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D007544:Isopropyl Thiogalactoside; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics; D013482:Superoxide Dismutase / Q000096:biosynthesis* / Q000235:genetics*
D011994:Recombinant Proteins; D007544:Isopropyl Thiogalactoside; D013482:Superoxide Dismutase