The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation

Biochemical and Biophysical Research Communications

Volumn 304, Issue 1, 2003, Pages 148-152

  Arakawa, Tsutomu ^a   Tsumoto, Kouhei ^b  

^a ALLIANCE PROTEIN LABORATORIES   (United States)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

Aggregation; Arginine; Inclusion body; Refolding; Reversibility

Indexed keywords

ARGININE; PROTEIN;

ARTICLE; HEAT TREATMENT; MELTING POINT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMOSTABILITY;

EID: 0037466513     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00578-3     Document Type: Article

References (17)

1. Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56.
2. Clark E.D.B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9:1998;157-163.
3. Misawa S., Kumagai I. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies. Biopolymers. 51:1999;297-307.
4. Tsumoto K., Ejima D., Kumagai I., Arakawa T. Practical considerations in refolding proteins from inclusion bodies. Protein Express. Purif. 28:2003;1-8.
5. Arora D., Khanna N. Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 52:1996;127-133.
6. Suenaga M., Ohmae H., Tsuji S., Itoh T., Nishimura O. Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation. Biotechnol. Appl. Biochem. 28:1998;119-124.
7. Rudolph R., Boehn G., Lilie H., Jaenicke R. Creighton T.E. A Practical Approach in Protein Function. second ed. 1997;57-99 IRL Press.
8. Brinkmann U., Buchner J., Pastan I. Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections. Proc. Natl. Acad. Sci. USA. 89:1992;3075-3079.
9. Buchner J., Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology. 9:1991;157-162.
10. Tsumoto K., Shinoki K., Kondo H., Uchikawa M., Juji T., Kumagai I. Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - application to a human single-chain Fv fragment. J. Immunol. Methods. 219:1998;119-129.
11. Asano R., Kudo T., Makabe K., Tsumoto K., Kumagai I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett. 528:2002;70-76.
12. Oneda H., Inouye K. Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli. J. Biochem. 126:1999;905-911.
13. Arakawa T., Bhat R., Timasheff S.N. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry. 29:1990;1924-1931.
14. Kita Y., Arakawa T., Lin T.Y., Timasheff S.N. Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry. 33:1994;15178-15189.
15. Arakawa T., Timasheff S.N. The stabilization of proteins by osmolytes. Biophys. J. 47:1985;411-414.
16. M. Umetsu, K. Tsumoto, M. Hara, K. Ashish, S. Goda, T. Adschri, I. Kumagai, How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system: spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment, J. Biol. Chem. 278 (2003) 8979-8987.
17. Shiraki K., Kudou M., Fujiwara S., Imanaka T., Takagi M. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem. 132:2002;591-595.