Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity
- Авторлар: Sharapov M.1, Novoselov V.1, Ravin V.1
-
Мекемелер:
- Institute of Cell Biophysics
- Шығарылым: Том 81, № 4 (2016)
- Беттер: 420-427
- Бөлім: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150850
- DOI: https://doi.org/10.1134/S0006297916040131
- ID: 150850
Дәйексөз келтіру
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.
Негізгі сөздер
Авторлар туралы
M. Sharapov
Institute of Cell Biophysics
Хат алмасуға жауапты Автор.
Email: sharapov.mars@gmail.com
Ресей, Pushchino, Moscow Region, 142290
V. Novoselov
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Ресей, Pushchino, Moscow Region, 142290
V. Ravin
Institute of Cell Biophysics
Email: sharapov.mars@gmail.com
Ресей, Pushchino, Moscow Region, 142290
![](/img/style/loading.gif)