Purification of recombinant ovalbumin from inclusion bodies of Escherichia coli

Protein Expression and Purification

Volumn 117, Issue , 2016, Pages 52-58

  Upadhyay, Vaibhav ^a   Singh, Anupam ^a   Panda, Amulya K ^a  

^a NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

Author keywords

Inclusion bodies; Ovalbumin; Refolding and purification; Solubilization

Indexed keywords

OVALBUMIN; RECOMBINANT PROTEIN;

CELL INCLUSION; CHEMISTRY; ESCHERICHIA COLI; ISOLATION AND PURIFICATION; PROTEIN REFOLDING;

ESCHERICHIA COLI; INCLUSION BODIES; OVALBUMIN; PROTEIN REFOLDING; RECOMBINANT PROTEINS;

EID: 84958894681     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2015.09.015     Document Type: Article

References (35)

1. L.T. Hunt, and M.O. Dayhoff A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha1-proteinase inhibitor Biochem. Biophys. Res. Commun. 95 1980 864 871
2. J.A. Huntington, and P.E. Stein Structure and properties of ovalbumin J. Chromatogr. B Biomed. Sci. Appl. 756 2001 189 198
3. H.L. Sharp, R.A. Bridges, W. Krivit, and E.F. Freier Cirrhosis associated with alpha-1-antitrypsin deficiency: a previously unrecognized inherited disorder J. Lab. Clin. Med. 73 1969 934 939
4. R.L. Davis, A.E. Shrimpton, P.D. Holohan, C. Bradshaw, D. Feiglin, G.H. Collins, P. Sonderegger, J. Kinter, L.M. Becker, F. Lacbawan, D. Krasnewich, M. Muenke, D.A. Lawrence, M.S. Yerby, C.M. Shaw, B. Gooptu, P.R. Elliott, J.T. Finch, R.W. Carrell, and D.A. Lomas Familial dementia caused by polymerization of mutant neuroserpin Nature 401 1999 376 379
5. M. Yamasaki, W. Li, D.J. Johnson, and J.A. Huntington Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization Nature 455 2008 1255 1258
6. J.A. Huntington, T.J. Sendall, and M. Yamasaki New insight into serpin polymerization and aggregation Prion 3 2009 12 14
7. A.S. Knaupp, V. Levina, A.L. Robertson, M.C. Pearce, and S.P. Bottomley Kinetic instability of the serpin Z α1-antitrypsin promotes aggregation J. Mol. Biol. 396 2010 375 383
8. D.A. Lomas, D.L. Evans, J.T. Finch, and R.W. Carrell The mechanism of Z α1-antitrypsin accumulation in the liver Nature 357 1992 605 607
9. H. Azakami, A. Mukai, and A. Kato Role of amyloid type cross β-structure in the formation of soluble aggregate and gel in heat-induced ovalbumin J. Agric. Food Chem. 53 2005 1254 1257
10. F.G. Pearce, S.H. Mackintosh, and J.A. Gerrard Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing J. Agric. Food Chem. 55 2007 318 322
11. N. Tanaka, Y. Morimoto, Y. Noguchi, T. Tada, T. Waku, S. Kunugi, T. Morii, Y.F. Lee, T. Konno, and N. Takahashi The mechanism of fibril formation of a non-inhibitory serpin ovalbumin revealed by the identification of amyloidogenic core regions J. Biol. Chem. 286 2011 5884 5894
12. S.L. Myers, N.H. Thomson, S.E. Radford, and A.E. Ashcroft Investigating the structural properties of amyloid-like fibrils formed in vitro from β2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry Rapid Commun. Mass Spectrom. 20 2006 1628 1636
13. E. Frare, M.F. Mossuto, P. Polverino de Laureto, M. Dumoulin, C.M. Dobson, and A. Fontana Identification of the core structure of lysozyme amyloid fibrils by proteolysis J. Mol. Biol. 361 2006 551 561
14. A. Nazabal, M.L. Maddelein, M. Bonneu, S.J. Saupe, and J.M. Schmitter Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry J. Biol. Chem. 280 2005 13220 13228
15. C. Scavenius, S. Ghodke, D.E. Otzen, and J.J. Enghild Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis Int. J. Mass Spectrom. 302 2011 167 173
16. J.H. Ippel, A. Olofsson, J. Schleucher, E. Lundgren, and S.S. Wijmenga Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy Proc. Natl. Acad. Sci. U.S.A. 99 2002 8648 8653
17. 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy Biochemistry 44 2005 4434 4441
18. M. Hoshino, H. Katou, Y. Hagihara, K. Hasegawa, H. Naiki, and Y. Goto Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange Nat. Struct. Biol. 9 2002 332 336
19. R.R. Burgess Refolding solubilized inclusion body proteins Methods Enzymol. 463 2009 259 282
20. A.K. Patra, R. Mukhopadhyay, R. Mukhija, A. Krishnan, L.C. Garg, and A.K. Panda Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli Protein Expr. Purif. 18 2000 182 192
21. S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310
22. A.K. Upadhyay, A. Murmu, A. Singh, and A.K. Panda Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli PLoS ONE 7 2012 e33951
23. R. Rudolph, and H. Lilie In vitro folding of inclusion body proteins FASEB J. 10 1996 49 56
24. E.D.B. Clark Refolding of recombinant proteins Curr. Opin. Biotechnol. 9 1998 157 163
25. F.A. Marston, and D.L. Hartley Solubilization of protein aggregates Methods Enzymol. 182 1990 264 276
26. T. Ishimaru, K. Ito, M. Tanaka, S. Tanaka, and N. Matsudomi The role of the disulfide bridge in the stability and structural integrity of ovalbumin evaluated by site-directed mutagenesis Biosci. Biotechnol. Biochem. 75 2011 544 549
27. N. Takahashi, T. Orita, and M. Hirose Production of chicken ovalbumin in Escherichia coli Gene 161 1995 211 216
28. S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
29. J. Hellman, P. Lassila, and P. Mantsala In vitro refolding of cyclomaltodextrin glucanotransferase from cytoplasmic inclusion bodies formed upon expression in Escherichia coli Protein Expr. Purif. 6 1995 56 62
30. M. Ling, M. Zou, M. Xu, J. Wang, and X. Ma Purification of recombinant human granulocyte-macrophage colony stimulating factor expressed in Escherichia coli Chin. J. Biotechnol. 11 1995 157 162
31. P.F. Wang, W.R. Novak, J.S. Cantwell, P.C. Babbitt, M.J. McLeish, and G.L. Kenyon Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies Protein Expr. Purif. 26 2002 89 95
32. J. Stockel, K. Doring, J. Malotka, F. Jahnig, and K. Dornmair Pathway of detergent-mediated and peptide ligand-mediated refolding of hetero dimeric class II major histocompatibility complex (MHC) molecules Eur. J. Biochem. 248 1997 684 691
33. R.R. Burgess Purification of overproduced Escherichia coli RNA polymerase σ factors by solubilizing inclusion bodies and refolding from sarkosyl Methods Enzymol. 273 1996 145 149
34. S.M. Singh, A. Sharma, A.K. Upadhyay, A. Singh, L.C. Garg, and A.K. Panda Solubilization of inclusion body proteins using n-propanol and its refolding into bioactive form Protein Expr. Purif. 81 2012 75 82
35. S. Jevsevar, V. Gaberc-Porekar, I. Fonda, B. Podobnik, J. Grdadolnik, and V. Menart Production of nonclassical inclusion bodies from which correctly folded protein can be extracted Biotechnol. Prog. 21 2005 632 639