Immobilized β-cyclodextrin polymer coupled to agarose gel properly refolding recombinant Staphylococcus aureus elongation factor-G in combination with detergent micelle

Protein Expression and Purification

Volumn 45, Issue 1, 2006, Pages 72-79

  Li, Jing Jing ^a   Venkataramana, Musturi ^b   Sanyal, Suparna ^b   Janson, Jan Christer ^b   Su, Zhi Guo ^a  

^a INSTITUTE OF PROCESS ENGINEERING   (China)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Cyclodextrin polymer; Chaperone; EF G; Immobilization; Protein refolding

Indexed keywords

BETA CYCLODEXTRIN DERIVATIVE; ELONGATION FACTOR G; OCTOXINOL; POLYMER; RECOMBINANT PROTEIN; SEPHAROSE;

AGAR GEL ELECTROPHORESIS; ARTICLE; CHEMISTRY; ISOLATION AND PURIFICATION; METHODOLOGY; MICELLE; PROTEIN FOLDING; STAPHYLOCOCCUS AUREUS; SYNTHESIS; TIME;

BETA-CYCLODEXTRINS; ELECTROPHORESIS, AGAR GEL; MICELLES; OCTOXYNOL; PEPTIDE ELONGATION FACTOR G; POLYMERS; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEPHAROSE; STAPHYLOCOCCUS AUREUS; TIME FACTORS;

STAPHYLOCOCCUS AUREUS;

EID: 28844495520     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.05.006     Document Type: Article

References (16)

1. B. Fischer, I. Sumner, and P. Goodenough Isolation and renaturation of bioactive proteins expressed in Escherichia coli as inclusion bodies Arzneimittelforschung 42 1992 1512 1515
2. P.Y. Shi, N. Maizels, and A.M. Weiner Recovery of soluble, active recombinant protein from inclusion bodies Biotechniques 23 1997 1036 1038
3. D. Hevehan, and E. De Bernardez Clark, oxidative renaturation of hen egg-white lysozyme. folding vs aggregation Biotechnol. Bioeng. 54 1997 221 228
4. V.R. Agashe, and F.U. Hartl Roles of molecular chaperones in cytoplasmic protein folding Semin. Cell Dev. Biol. 11 2000 15 25
5. R.J. Ellis Introduction -10 years of molecular chaperones Semin. Cell Dev. Biol. 11 2000 1 5
6. J.S. Weissmann, C.M. Hohl, O. Kovalenko, Y. Kashi, S. Chen, K. Braig, H.R. Saibil, W.A. Fenton, and A.L Horwich Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES Cell 83 1995 577 587
7. D. Rozema, and S.H. Gellman Artificial chaperones: protein refolding via sequential use of detergent and cyclodextrin J. Am. Chem. Soc. 117 1995 2373 2374
8. D. Rozema, and S.H. Gellman Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation Biochemistry 35 1996 15760 15771
9. D. Rozema, and S.H. Gellman Artificial chaperone-assisted refolding of carbonic anhydrase B J. Biol. Chem. 271 1996 3478 3487
10. D.L. Daugherty, D. Rozema, P.E. Hanson, and S.H. Gellman Artificial chaperone-assisted refolding of citrate synthase J. Biol. Chem. 273 1998 33961 33971
11. S.C. Sivakama, B. Raman, and D. Balasubramanian Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains- a sweet route to the native state of globular proteins FEBS Lett. 443 1999 215 219
12. N. Yuta, I. Masahiro, Y. Nozomi, A. Yasuhiro, and A. Kazunari Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone FEBS Lett. 553 2003 271 276
13. T. Mannen, S. Yamaguchi, J. Honda, S. Sugimoto, and T. Nagamune Expanded-bed protein refolding using a solid-phase artificial chaperone J. Biosci. Bioeng. 91 2001 403 408
14. G.E.S. Lindgren, Method for binding to polymers, International Patent, WO 9404192, 1994.
15. I. Nagaev, J. Bjorkman, D.I. Andersson, and D. Hughes Biological cost and compensatory evolution in fusidic acid-resistant Staphylococcus aureus Mol. Microbiol. 40 2001 433 439
16. J.J. Li, M. Venkataramana, A.Q. Wang, S. Sanyal, J.C. Janson, and Z.G. Su A mild hydrophobic interaction chromatography involving polyethylene glycol immobilized to agarose media refolding recombinant Staphylococcus aureus elongation factor G Protein Expr. Purif. 40 2005 327 335