Protein refolding for industrial processes

Current Opinion in Biotechnology

Volumn 12, Issue 2, 2001, Pages 202-207

  Clark, Eliana De Bernardez ^a  

^a Tufts University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PROTEIN;

CELL INCLUSION; CONTROLLED STUDY; COST; DISULFIDE BOND; HUMAN; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN RENATURATION; REVIEW; SOLUBILIZATION;

EID: 0035313135     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(00)00200-7     Document Type: Review

References (40)

1. Recombinant protein expression in Escherichia coli
2. Advances in refolding of proteins produced in E. coli
3. Refolding of recombinant proteins
4. In vitro folding of inclusion body proteins on an industrial scale
5. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies
6. Isolating inclusion bodies from bacteria
7. Protein aggregation: Folding aggregates, inclusion bodies and amyloid
8. Fourier transformed infrared spectroscopy in analysis of protein deposits
9. Inhibition of aggregation side reactions during in vitro protein folding
10. Inclusion body purification and protein refolding using microfiltration and size exclusion chromatography
11. Renaturation of heterodimeric platelet-derived growth factor from inclusion bodies of recombinant Escherichia coli using size-exclusion chromatography
12. Renaturation of 1-aminocyclopropane-1-carboxylate synthase expressed in Escherichia coli in the form of inclusion bodies into a dimeric and catalytically active enzyme
13. Refolding and purification of a urokinase plasminogen activator fragment by chromatography
14. Renaturation of Escherichia coli-derived recombinant human macrophage colony stimulating factor
15. Production of antifungal recombinant peptides in Escherichia coli
16. High-level expression of the endo-β-N-acetylglucosaminidase F2 gene in E. coli: One step purification to homogeneity
17. Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli
18. Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
19. Effects of operating parameters in in vitro renaturation of a fusion protein of human growth hormone and glutathione S-transferase from inclusion body
20. Artificial chaperone-assisted refolding of citrate synthase
21. Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains - A sweet route to the native structure of globular proteins
22. Cycloamylose as an efficient artificial chaperone for protein refolding
23. Reversible protection of disulfide bonds followed by oxidative folding render recombinant hCGβ highly immunogenic
24. Convenient and efficient in vitro folding of disulfide containing globular protein from crude bacterial inclusion bodies
25. High pressure fosters protein refolding from aggregates at high concentration
26. Continuous refolding of lysozyme with fed-batch addition of denatured protein solution
27. Production of leptin in Escherichia coli: A comparison of methods
28. Improved protein refolding using hollow-fibre membrane dialysis
29. Refolding of low molecular weight urokinase plasminogen activator by dilution and size exclusion chromatography - A comparative study
30. Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography
31. Matrix-assisted folding of single-chain Fv cellulose binding domain fusion proteins
32. Inhibition of stress-induced aggregation of protein therapeutics
33. Oxidative renaturation of hen egg-white lysozyme. Folding vs aggregation
34. A small-molecule catalyst of protein folding in vitro and in vivo
35. BIP and PDI cooperate in the oxidative folding of antibodies in vitro
36. Oxidative refolding chromatography: Folding of the scorpion toxin Cn5
37. Design of a molecular chaperone-assisted protein folding bioreactor
38. Hydrostatic pressure rescues native protein from aggregates
39. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure