Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity
- Authors: Sharapov M.G.1, Novoselov V.I.1, Ravin V.K.1
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Affiliations:
- Institute of Cell Biophysics
- Issue: Vol 81, No 4 (2016)
- Pages: 420-427
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150850
- DOI: https://doi.org/10.1134/S0006297916040131
- ID: 150850
Cite item
Abstract
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.
About the authors
M. G. Sharapov
Institute of Cell Biophysics
Author for correspondence.
Email: sharapov.mars@gmail.com
Russian Federation, Pushchino, Moscow Region, 142290
V. I. Novoselov
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Russian Federation, Pushchino, Moscow Region, 142290
V. K. Ravin
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Russian Federation, Pushchino, Moscow Region, 142290
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