Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity
- Авторы: Sharapov M.1, Novoselov V.1, Ravin V.1
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Учреждения:
- Institute of Cell Biophysics
- Выпуск: Том 81, № 4 (2016)
- Страницы: 420-427
- Раздел: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150850
- DOI: https://doi.org/10.1134/S0006297916040131
- ID: 150850
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Аннотация
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.
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Об авторах
M. Sharapov
Institute of Cell Biophysics
Автор, ответственный за переписку.
Email: sharapov.mars@gmail.com
Россия, Pushchino, Moscow Region, 142290
V. Novoselov
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Россия, Pushchino, Moscow Region, 142290
V. Ravin
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Россия, Pushchino, Moscow Region, 142290