Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity


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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.

作者简介

M. Sharapov

Institute of Cell Biophysics

编辑信件的主要联系方式.
Email: sharapov.mars@gmail.com
俄罗斯联邦, Pushchino, Moscow Region, 142290

V. Novoselov

Institute of Cell Biophysics

Email: sharapov.mars@gmail.com
俄罗斯联邦, Pushchino, Moscow Region, 142290

V. Ravin

Institute of Cell Biophysics

Email: sharapov.mars@gmail.com
俄罗斯联邦, Pushchino, Moscow Region, 142290


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