中国生物工程杂志

Peroxiredoxin (Prx), one of the ubiquitous enzymes in organisms, plays an important role in eliminating oxidative stress. The cDNA encoding peroxiredoxin(Prx) of Fenneropenaeus chinensis protein was cloned and expressed in E. coli. The recombinant protein was expressed as inclusion body after IPTG induced. LC–ESI–MS analysis showed that four peptide fragments of the recombinant protein were identical to the corresponding sequence of F. chinensis Prx. The fusion protein was purified using the immobilized-metal affinity chromatography. After refolded, the purified recombinant protein was shown to reduce H2O2 in the presence of dithiothreitol. The fusion protein is useful for studies on the function of Prx in immune defense and against oxidative stress of F. chinensis.