Expression and culture optimization of mini-chaperone GroEL (191-345) in E. coli
The apical domain of GroEL (residues 191-345) is expressed in E. coli to give a functional mini-chaperone, and the refolding yields of scorpion toxin Cn5, cyclophilin A and IGPS assisted by mini-chaperone were improved remarkably. Owing to its potentially broad application, the optimum culture condi...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Zhejiang University Press
2003-11-01
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| Series: | 浙江大学学报. 农业与生命科学版 |
| Subjects: | |
| Online Access: | https://www.academax.com/doi/10.3785/1008-9209.2003.06.0603 |
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| Summary: | The apical domain of GroEL (residues 191-345) is expressed in E. coli to give a functional mini-chaperone, and the refolding yields of scorpion toxin Cn5, cyclophilin A and IGPS assisted by mini-chaperone were improved remarkably. Owing to its potentially broad application, the optimum culture condition of mini-chaperone was studied in detail. M9 medium with carbon source and inorganic salts was found to be suitable for the expression of mini-chaperone GroEL (191-345) in E. coli. M9 medium was then reformulated and the optimum temperature, oxygen demand and induction conditions were carefully chosen to improve the mini-chaperone production to 556.3 mg/L. |
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| ISSN: | 1008-9209 2097-5155 |