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Literature DB >> 14680955

In vitro protein refolding by chromatographic procedures.

Ming Li¹, Zhi-Guo Su, Jan-Christer Janson.

Abstract

In vitro protein refolding is still a bottleneck in both structural biology and in the development of new biopharmaceuticals, especially for commercially important polypeptides that are overexpressed in Escherichia coli. This review focuses on protein refolding methods based on column procedures because recent advances in chromatographic refolding have shown promising results.

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Year: 2004 PMID： 14680955 DOI： 10.1016/j.pep.2003.08.023

Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650

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Cited

19 in total

1. Localization of functional polypeptides in bacterial inclusion bodies.

Authors: Elena García-Fruitós; Anna Arís; Antonio Villaverde
Journal: Appl Environ Microbiol Date: 2006-11-03 Impact factor: 4.792

Review 2. Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli.

Authors: Chunfang Ling; Junyan Zhang; Deqiu Lin; Ailin Tao
Journal: World J Microbiol Biotechnol Date: 2015-03-20 Impact factor: 3.312

3. Ternary system of solution additives with arginine and salt for refolding of beta-galactosidase.

Authors: Akiko Fujimoto; Atsushi Hirano; Kentaro Shiraki
Journal: Protein J Date: 2010-04 Impact factor: 2.371

4. Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli.

Authors: Shivcharan Prasad; Prashant B Khadatare; Ipsita Roy
Journal: Appl Environ Microbiol Date: 2011-05-06 Impact factor: 4.792

5. L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.

Authors: Venugopal Gunda; Chandra Shekhar Boosani; Raj Kumar Verma; Chittibabu Guda; Yakkanti Akul Sudhakar
Journal: Protein Pept Lett Date: 2012-10 Impact factor: 1.890

In vitro protein refolding by chromatographic procedures.

1. Localization of functional polypeptides in bacterial inclusion bodies.

Review 2. Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli.

3. Ternary system of solution additives with arginine and salt for refolding of beta-galactosidase.

4. Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli.

5. L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.

6. The pilot-scale preparation of the SA-hGM-CSF bi-functional fusion protein.

Review 7. Overcoming the Solubility Problem in E. coli: Available Approaches for Recombinant Protein Production.

8. An automatic refolding apparatus for preparative-scale protein production.

9. Purification and Refolding of Overexpressed Human Basic Fibroblast Growth Factor in Escherichia coli.

10. An account on the innovative path of cooperation with Prof. Zhiguo Su in bioseparation.