А New Program for Detecting Geometrical Core of a Set of Structures of Macromolecular Complexes
A genetically engineered construct was created encoding a chimeric enzyme consisting of human peroxiredoxin 6 and E. coli manganese superoxide dismutase. Conditions for synthesis of the chimeric protein in E. coli cells were optimized. It was found that the synthesis of enzymes in the form of a single polypeptide chain with peroxiredoxin 6 sequence from the N-terminus and manganese superoxide dismutase from the C-terminus (PSH) does not affect their enzymatic activity. On the contrary, when manganese superoxide dismutase is located from the N-terminus, while peroxiredoxin 6 resides at the C-terminus (SPH), the enzyme could not be obtained in a water-soluble and active form. An active chimeric protein (PSH) was obtained, possessing a combination of peroxidase and superoxide dis- mutase activities, and its physicochemical properties were studied. The therapeutic activity of chimeric protein PSH was shown using rat models of artificial oxidative stress: ischemia/reperfusion of the kidney and heart, and chemical burn of the upper respiratory tract.