A comparative analysis of rapid methods for purification and refolding of recombinant bovine prion protein

Protein Expression and Purification

Volumn 82, Issue 2, 2012, Pages 380-388

  Vrentas, Catherine E ^a   Onstot, Stephanie ^a   Nicholson, Eric M ^a  

^a NATIONAL ANIMAL DISEASE CENTER   (United States)

Author keywords

Encephalopathy; Inclusion body; Prion; PrP; Purification; Recombinant

Indexed keywords

BUFFER; COBALT; RECOMBINANT PROTEIN;

AFFINITY CHROMATOGRAPHY; ANIMAL; ARTICLE; CATTLE; CELL INCLUSION; CHEMISTRY; COMPARATIVE STUDY; ISOLATION AND PURIFICATION; PRION; PROTEIN BINDING; PROTEIN REFOLDING; PROTEIN SECONDARY STRUCTURE;

ANIMALS; BUFFERS; CATTLE; CHROMATOGRAPHY, AFFINITY; COBALT; INCLUSION BODIES; PRIONS; PROTEIN BINDING; PROTEIN REFOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI;

EID: 84857946329     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2012.02.008     Document Type: Article

References (18)

1. A. Negro, V. De Filippis, S.D. Skaper, P. James, and M.C. Sorgato The complete mature bovine prion protein highly expressed in Escherichia coli: biochemical and structural studies FEBS Lett. 412 1997 359 364
2. N. Makarava, and I.V. Baskakov Expression and purification of full-length recombinant PrP of high purity A.F. Hill, Prion Protein Protocols, Methods in Molecular Biology vol. 459 2008 Humana Press Totowa, NJ 131 143
3. S.M. Yin, Y. Zheng, and P. Tien On-column purification and refolding of recombinant bovine prion protein: using its octapeptide repeat sequences as a natural affinity tag Protein Expr. Purif. 32 2003 104 109
4. H. Rezaei, D. Marc, Y. Choiset, M. Takahashi, G.H.B. Hoa, and T. Haertle High yield purification and physio-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility Eur. J. Biochem. 267 2000 2833 2839
5. O. Andrievskaia, H. McRae, C. Elmgren, H. Huang, A. Balachandran, and K. Nielsen Generation of antibodies against bovine recombinant prion protein in various strains of mice Clin. Vaccine Immunol. 13 2006 98 105
6. C. Treiber, A.R. Thompsett, R. Pipkorn, D.R. Brown, and G. Multhaup Real-time kinetics of discontinuous and highly conformational metal-ion binding sites of prion protein J. Biol. Inorg. Chem. 12 2007 711 720
7. J.A. Bornhorst, and J.J. Falke Purification of proteins using polyhistidine affinity tags Methods Enzymol. 326 2000 245 254
8. L. Pagliato, A. Negri, S. Nonnis, F. Taverna, L. Sangiorgio, S. Ronchi, and G. Tedeschi Prion protein from Xenopus laevis: overexpression in Escherichia coli of the His-tagged protein and production of polyclonal antibodies Protein Expr. Purif. 46 2006 489 494
9. G.S. Jackson, A.F. Hil, C. Joseph, L. Hosszu, A. Power, J.P. Waltho, A.R. Clarke, and J. Collinge Multiple folding pathways for heterologously expressed human prion protein Biochim. Biophys. Acta. 1431 1999 1 13
10. Available from: < http://www.invitrogen.com/site/us/en/home/ References/Molecular-Probes-The-Handbook/Thiol-Reactive-Probes/ Introduction-to-Thiol-Modification-and-Detection.html > (accessed 12.12.11).
11. O. Julien, S. Chatterjee, T.C. Bjorndahl, B. Sweeting, S. Acharya, and V. Semenchenko Relative and regional stabilities of the hamster, mouse, rabbit, and bovine proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies Biochemistry 50 2011 7536 7545
12. N. Oganesyan, S.-H. Kim, and R. Kim On-column refolding of proteins PharmaGenomics 2004 22 25
13. X.-Y. Dong, L.-J. Chen, and Y. Sun Refolding and purification of histidine-tagged protein by artificial chaperone-assisted metal affinity chromatography J. Chromatogr. A. 1216 2009 5207 5213
14. P. Pergami, H. Jaffe, and J. Safar Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form Anal. Biochem. 236 1996 63 73
15. L. Breydo, O.V. Bocharova, N. Makarava, V.V. Salnikov, M. Anderson, and I. Baskakov Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase-K resistant conformation Biochemistry 44 2005 15534 15543
16. S. Hornemann, C. Korth, B. Oesch, R. Riek, G. Wider, K. Wuthrich, and R. Glockshuber Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization FEBS Lett. 413 1997 277 281
17. A. Pavlicek, L. Bednarova, and K. Holada Production, purification, and oxidative folding of the mouse recombinant prion protein Folia Microbiol. 52 2007 391 397
18. R. Zahn, C. von Schroetter, and K. Wuthrich Human prion proteins expressed in Escherichia coli and purified by high affinity column refolding FEBS Lett. 417 1997 400 404