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A chimeric gene construct encoding human peroxiredoxin 6 and Mn-superoxide dismutase from
Escherichia coli
was developed. Conditions for expression of the fusion protein in
E. coli
cell were optimized. Fusing of the enzymes into a single polypeptide chain with peroxiredoxin 6 at the
N
-terminus (PSH) did not affect their activities. On the contrary, the chimeric protein with reverse order of enzymes (SPH) was not obtained in a water-soluble active form. The active chimeric protein (PSH) exhibiting both peroxidase and superoxide dismutase activities was prepared and its physicochemical properties were characterized.