ABSTRACT
ABSTRACT: Glutathione peroxidase 4 (GPx4) is a critical selenoenzyme which could reduce hydrogen peroxide, membrane-bound phospholipid and cholesterol hydroperoxides. However, it has been dicult to produce recombinant human GPx4 (hGPx4) in E. coli for a long time due to the complicated expression mechanism of selenocysteine (Sec)-containing protein. In this study, seleno-hGPx4 mutant was expressed in an E. coli BL21(DE3)cys auxotrophic strain and the kinetics of recombinant hGPx4 mutant based on H2O2 was studied. The results shows that the mutant exhibited a typical “ping-pong” mechanism, which is similar to native GPx4. It provides an important theoretical foundation to study the recombinant GPx produced in E.coli.
