Renaturation of reduced ribonuclease A with a microsphere-induced refolding system

Biotechnology Progress

Volumn 16, Issue 2, 2000, Pages 248-253

  Shimizu, Hidenobu ^a   Fujimoto, Keiji ^a   Kawaguchi, Haruma ^a  

^a KEIO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DITHIOTHREITOL; POLYMERIC MICROSPHERES; RIBONUCLEASES;

ADSORPTION; DISULFIDE BOND; DITHIOTHREITOL; ENZYME ACTIVITY; ENZYME RENATURATION; MICROSPHERE; POLYMER; PROTEIN FOLDING; PROTEIN IMMOBILIZATION; REACTION TIME; RENATURATION; RIBONUCLEASE A;

ADSORPTION; BIOMATERIALS; ENZYME IMMOBILIZATION; ENZYME KINETICS; INTERFACES (MATERIALS); PLASTIC PRODUCTS; REACTION KINETICS; RNA; SURFACE PHENOMENA;

GENETIC ENGINEERING;

BIOCHEMISTRY; DITHIOTHREITOL; MICROSPHERES; PROTEIN FOLDING; PROTEIN RENATURATION; RIBONUCLEASE, PANCREATIC; SURFACE PROPERTIES;

EID: 0034009142     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp000008c     Document Type: Article

References (27)

1. Marston, F. A. O. The Purification of Eukaryotic Polypeptides Synthesized in Escherichia coli. Biochem. J. 1986, 240, 1-12.
2. Schein, C. H. Production of Soluble Recombinant Proteins in Bacteria. Bio/Technology 1989, 7, 1141-1149.
3. Goldberg, M. E.; Rudolph, R.; Jaenicke, R. A Kinetic Study of Competition between Renaturation and Aggregation during the Refolding of Denatured-Reduced Egg White Lysozyme. Biochemistry 1991, 30, 2790-2797.
4. Cleland, J. L. Impact of Protein Folding on Biotechnology. In Protein Folding; Cleland, J. L., Ed.; ACS Symposium Series; American Chemical Society: Washington, DC; 1993, pp 1-21.
5. Zardeneta, G.; Horowitz, P. M. Detergent, Liposome, and Micelle-Assisted Protein Refolding. Anal. Biochem. 1994, 223, 1-6.
6. Sadana, A. Protein Refolding and Inactivation During Bioseparation: Bioprocessing Implications. Biotechnol. Bioeng. 1995, 48, 481-489.
7. Rudolph, R.; Lilie, H. In Vitro Folding of Inclusion Body Proteins. FASEB J. 1996, 10, 49-56.
8. Batas, B.; Chaudhuri, J. B. Protein Refolding at High Concentration Using Size-Exclusion Chromatography. Biotechnol. Bioeng. 1996, 50, 16-23.
9. West, S. W.; Chaudhuri, J. B.; Howell, J. A. Improved Protein Refolding Using Hollow-Fibre Membrane Dialysis. Biotechnol. Bioeng. 1998, 57, 590-599.
10. Hanson, P. E.; Gellman, S. H. Mechanistic Comparison of Artificial-Chaperone-Assisted and Unassisted Refolding of Urea-Denatured Carbonic Anhydrase B. Fold. Des. 1998, 3, 457-468.
11. Shimizu, H.; Fujimoto, K.; Kawaguchi, H. Refolding of Protein Using Thiol-Carrying Latex Particles. Colloids Surf., A 1999, 753, 421-427.
12. Inomata, Y.; Wada, T.; Handa, H.; Fujimoto K.; Kawaguchi, H. Purification of DNA-Carrying Affinity Latex and Purification of Transcription Factors with the Latex. J. Biomat. Sci. Polym. Ed. 1994, 5, 293-302.
13. Ellman, G. L. Tissue Sulfhydryl Groups. Arch. Biochem. Biophys. 1959, 82, 70-77.
14. Lyles, M. M.; Gilbert, H. F. Catalysis of the Oxidative Folding of Ribonuclease A by Protein Disulfide Isomerase: Dependence of the Rate on the Composition of the Redox Buffer. Biochemistry 1991, 30, 613-619.
15. Hagen, A. J.; Hatten, T. A.; Wang, D. I. C. Protein Refolding in Reversed Micelles. Biotechnol. Bioeng. 1990, 35, 955-965.
16. Morjana, N. A.; Gilbert, H. F. Catalysis of Protein Folding by Agarose-Immobilized Protein Disulfide Isomerase. Protein Expression Purif. 1994, 5, 144-148.
17. Anfinsen, C. B.; Haber, E. Studies on the Reduction and Re-formation of Protein Disulfide Bonds. J. Biol. Chem. 1961, 236, 1361-1363.
18. Thannhauser, T. W.; Konishi, Y.; Scheraga, H. A. Sensitive Quantitative Analysis of Disulfide Bonds in Polypeptides and Proteins. Anal. Biochem. 1984, 138, 181-188.
19. Gething, M.-J.; Sambrook, J. Protein Folding in the Cell. Nature 1992, 355, 33-45.
20. Hartl, F. U. Molecular Chaperones in Cellular Protein Folding. Nature 1996, 381, 571-580.
21. Freedman, R. B. Protein Disulfide Isomerase: Multiple Roles in the Modification of Nascent Secretory Proteins. Cell 1989, 57, 1069-1072.
22. Noiva, R.; Lennarz, W. J. Protein Disulfide Isomerase: A Multifunctional Protein Resident in the Lumen of the Endoplasmic Reticulum. J. Biol. Chem. 1992, 267, 3553-3556.
23. Gilbert, H. F. Protein Disulfide Isomerase and Assisted Protein Folding. J. Biol. Chem. 1997, 272, 29399-29402.
24. Saxena, V. P.; Wetlaufer, D. B. Formation of Three-Dimensional Structure in Proteins. I. Rapid Nonenzymic Reactivation of Reduced Lysozyme. Biochemistry 1970, 9, 5015-5023.
25. Hwang, C.; Sinskey, A. J.; Lodish, H. F. Oxidized Redox State of Glutathione in the Endoplasmic Reticulum. Science 1992, 257, 1496-1502.
26. Konishi, Y.; Ooi, T.; Scheraga, H. A. Regeneration of Ribonuclease A from the Reduced Protein. Rate-Limiting Steps. Biochemistry 1982, 21, 4734-4740.
27. Creighton, T. E. Intermediates in the Refolding of Reduced Ribonuclease A. J. Mol. Biol. 1979, 129, 411-431.