Refolding and simultaneous purification by three-phase partitioning of recombinant proteins from inclusion bodies

Protein Science

Volumn 17, Issue 11, 2008, Pages 1987-1997

  Raghava, Smita ^a   Barua, Bipasha ^b   Singh, Pradeep K ^a   Das, Mili ^b   Madan, Lalima ^b   Bhattacharyya, Sanchari ^b   Bajaj, Kanika ^b   Gopal, B ^b   Varadarajan, Raghavan ^b   Gupta, Munishwar N ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

^b INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

CcdB mutants; Human CD4; Inclusion bodies; Protein refolding; Recombinant ribonuclease a; Three phase partitioning

Indexed keywords

RECOMBINANT PROTEIN;

ARTICLE; CELL INCLUSION; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION;

ANIMALS; ANTIGENS, CD4; BACTERIAL PROTEINS; BACTERIAL TOXINS; DROSOPHILA PROTEINS; ESCHERICHIA COLI; HUMANS; INCLUSION BODIES; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN TYROSINE PHOSPHATASES; RECOMBINANT PROTEINS; RIBONUCLEASE, PANCREATIC;

ESCHERICHIA COLI; EUKARYOTA;

EID: 55549091446     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.036939.108     Document Type: Article

References (39)

1. Armstrong, N., de Lencastre, A., and Gouaux, E. 1999. A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci. 8: 1475-1483.
2. Bajaj, K., Chakshusmathi, G., Bachhawat-Sikder, K., Surolia, A., and Varadarajan, R. 2004. Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein). Biochem. J. 380: 409-417.
3. Bajaj, K., Chakrabarti, P., and Varadarajan, R. 2005. Mutagenesis-based definitions and probes of residue burial in proteins. Proc. Natl. Acad. Sci. 102: 16221-16226.
4. Barth, S., Huhn, M., Matthey, B., Klimka, A., Galinski, E.A., and Engert, A. 2000. Compatible-solute-supported periplasmic expression of functional recombinant proteins under stress conditions. Appl. Environ. Microbiol. 66: 1572-1579.
5. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
6. Chakshusmathi, G., Mondal, K., Lakshmi, G.S., Singh, G., Roy, A., Ch, R.B., Madhusudhanan, S., and Varadarajan, R. 2004. Design of temperature-sensitive mutants solely from amino acid sequence. Proc. Natl. Acad. Sci. 101: 7925-7930.
7. Citovsky, V., Knorr, D., Schuster, G., and Zambryski, P. 1990. The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein. Cell 60: 637-647.
8. Connelly, P.R., Varadarajan, R., Sturtevant, J.M., and Richards, F.M. 1990. Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry. Biochemistry 29: 6108-6114.
9. Crook, E.M., Mathias, A.P., and Rabin, B.R. 1960. Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate. Biochem. J. 74: 234-238.
10. Dalgleish, A.G., Beverley, P.C., Clapham, P.R., Crawford, D.H., Greaves, M.F., and Weiss, R.A. 1984. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312: 763-767.
11. Das, M., Kobayashi, M., Yamada, Y., Sreeramulu, S., Ramakrishnan, C., Wakatsuki, S., Kato, R., and Varadarajan, R. 2007. Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts. J. Mol. Biol. 372: 1278-1292.
12. delCardayré, S.B., Ribo, M., Yokel, E.M., Quirk, D.J., Rutter, W.J., and Raines, R.T. 1995. Engineering ribonuclease A: Production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 8: 261-273.
13. Dennison, C. and Lovrien, R. 1997. Three phase partitioning: Concentration and purification of proteins. Protein Expr. Purif. 11: 149-161.
14. Doyle, C. and Strominger, J.L. 1987. Interaction between CD4 and class II MHC molecules mediates cell adhesion. Nature 330: 256-259.
15. Ganesh, C., Shah, A.N., Swaminathan, C.P., Surolia, A., and Varadarajan, R. 1997. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 36: 5020-5028.
16. Goldenberg, D.P. 1989. Analysis of protein conformation by gel electrophoresis. In Protein structure. A practical approach (ed. T.E. Creighton), pp. 225-250. Oxford University Press, UK.
17. Hofmann, A., Tai, M., Wong, W., and Glabe, C.G. 1995. A sparse matrix screen to establish initial conditions for protein renaturation. Anal. Biochem. 230: 8-15.
18. Jain, S., Singh, R., and Gupta, M.N. 2004. Purification of recombinant green fluorescent protein by three-phase partitioning. J. Chromatogr. A 1035: 83-86.
19. Kiss, E. and Borbas, R. 2003. Protein adsorption at liquid/liquid interface with low interfacial tension. Colloids Surf. B Biointerfaces 31: 169-176.
20. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
21. Laity, J.H., Shimotakahara, S., and Scheraga, H.A. 1993. Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli. Proc. Natl. Acad. Sci. 90: 615-619.
22. Lange, C., Patil, G., and Rudolph, R. 2005. Ionic liquids as refolding additives: N′-alkyl and N′-(ω-hydroxyalkyl) N-methylimidazolium chlorides. Protein Sci. 14: 2693-2701.
23. Lovrien, R.E., Conroy, M.J., and Richardson, T.I. 1995. Molecular basis for protein separations. In Protein-solvent interactions (ed. R.B. Gregory), pp. 521-553. Marcel Dekker, New York.
24. Madan, L.L. and Gopal, B. 2008. Addition of a polypeptide stretch at the N-terminus improves the expression, stability and solubility of recombinant protein tyrosine phosphatases from Drosophila melanogaster. Protein Expr. Purif. 57: 234-243.
25. Middelberg, A.P.J. 2002. Preparative protein refolding. Trends Biotechnol. 20: 437-443.
26. Misawa, S. and Kumagai, I. 1999. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies. Biopolymers 51: 297-307.
27. Okorokov, A.L., Panov, K.I., te Poele, R.H., Breukelman, H.J., Furia, A., Karpeisky, M., and Beintema, J.J. 1995. An efficient system for active bovine pancreatic ribonuclease expression in Escherichia coli. Protein Expr. Purif. 6: 472-480.
28. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4: 2411-2423.
29. Przybycien, T.M., Pujar, N.S., and Steele, L.M. 2004. Alternative bioseparation operations: Life beyond packed-bed chromatography. Curr. Opin. Biotechnol. 15: 469-478.
30. Rogl, H., Kosemund, K., Kuhlbrandt, W., and Collinson, I. 1998. Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography. FEBS Lett. 432: 21-26.
31. Schmid, F.X. 1989. Spectral methods of characterizing protein conformation and conformational changes. Oxford University Press, Oxford, UK.
32. Sharma, D., Balamurali, M.M., Chakraborty, K., Kumaran, S., Jeganathan, S., Rashid, U., Ingallinella, P., and Varadarajan, R. 2005. Protein minimization of the gp120 binding region of human CD4. Biochemistry 44: 16192-16202.
33. Stempfer, G., Holl-Neugebauer, B., and Rudolph, R. 1996. Improved refolding of an immobilized fusion protein. Nat. Biotechnol. 14: 329-334.
34. Tanimizu, N., Ueno, H., and Hayashi, R. 2002. Replacement of His12 or His119 of bovine pancreatic ribonuclease A with acidic amino acid residues for the modification of activity and stability. J. Biosci. Bioeng. 94: 39-44.
35. Taylor, G., Hoare, M., Gray, D.R., and Marston, F.A.O. 1986. Size and density of protein inclusion bodies. Biotechnology 43: 553-557.
36. Tsumoto, K., Ejima, D., Kumagai, I., and Arakawa, T. 2003. Practical considerations in refolding proteins from inclusion bodies. Protein Expr. Purif. 28: 1-8.
37. Van Melderen, L., Thi, M.H., Lecchi, P., Gottesman, S., Couturier, M., and Maurizi, M.R. 1996. ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271: 27730-27738.
38. Varadarajan, R., Sharma, D., Chakraborty, K., Patel, M., Citron, M., Sinha, P., Yadav, R., Rashid, U., Kennedy, S., Eckert, D., et al. 2005. Characterization of gp120 and its single-chain derivatives, gp120-CD4D12 and gp120-M9: Implications for targeting the CD4i epitope in human immunodeficiency virus vaccine design. J. Virol. 79: 1713-1723.
39. Wagner, A.P., Iordachel, M.C., and Wagner, L.P. 1983. A simple spectrophotometric method for the measurement of ribonuclease activity in biological fluids. J. Biochem. Biophys. Methods 8: 291-297.