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In vitro folding of inclusion body proteins
Abstract
Insoluble, inactive inclusion bodies are frequently formed upon recombinant protein production in transformed microorganisms. These inclusion bodies, which contain the recombinant protein in an highly enriched form, can be isolated by solid/liquid separation. After solubilization, native proteins can be generated from the inactive material by using in vitro folding techniques. New folding procedures have been developed for efficient in vitro reconstitution of complex hydrophobic, multidomain, oligomeric, or highly disulfíde‐bonded proteins. These protocols take into account process parameters such as protein concentration, catalysis of disulfide bond formation, temperature, pH, and ionic strength, as well as specific solvent ingredients that reduce unproductive side reactions. Modification of the protein sequence has been exploited to improve in vitro folding.—Rudolph, R., Lilie, H. In vitro folding of inclusion body proteins. FASEB J . 10, 49‐56.
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Cited by
Recombinant protein expression in Escherichia coli: advances and challenges
Rosano, G. L., & Ceccarelli, E. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00172 · Cited by 2,556
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0222-8 · Cited by 444
de Marco, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-26 · Cited by 367
Vallejo, L. F., & Rinas, U. (2004) · Microbial Cell Factories · doi:10.1186/1475-2859-3-11 · Cited by 311
Idicula‐Thomas, S., & Balaji, P. V. (2005) · Protein Science · doi:10.1110/ps.041009005 · Cited by 175
Metadata
- Authors
- Rudolph, R., & Lilie, H.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1996-01
- Volume
- 10
- Issue
- 1
- Pages
- 49-56
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1850804182
- Cited by
- 661
- References
- 0
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- closed
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