Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity
- 作者: Sharapov M.1, Novoselov V.1, Ravin V.1
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隶属关系:
- Institute of Cell Biophysics
- 期: 卷 81, 编号 4 (2016)
- 页面: 420-427
- 栏目: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150850
- DOI: https://doi.org/10.1134/S0006297916040131
- ID: 150850
如何引用文章
详细
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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