Physical-chemical features of non-detergent sulfobetaines active as protein-folding helpers

Biophysical Chemistry

Volumn 100, Issue 1-3, 2002, Pages 469-479

  Expert Bezançon, Nicole ^a   Rabilloud, Thierry ^b   Vuillard, Laurent ^c,d   Goldberg, Michel E ^a  

^a INSTITUT PASTEUR   (France)

^b CEA GRENOBLE   (France)

^c INSTITUT LAUE LANGEVIN   (France)

^d AVIDIS SA   (France)

Author keywords

Non detergent sulfobetaines; Physical chemical features; Protein folding helpers

Indexed keywords

BETA GALACTOSIDASE; BETAINE DERIVATIVE; BOVINE SERUM ALBUMIN; LYSOZYME; MONOCLONAL ANTIBODY; NON DETERGENT SULFOBETAINE; TRYPTOPHAN SYNTHASE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN RENATURATION; STRUCTURE ANALYSIS; SYNTHESIS;

BOVINAE;

EID: 0037438709     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00299-5     Document Type: Article

References (21)

1. Burton S.J., Quirk A.V., Wood P.C. Refolding human serum albumin at relatively high protein concentration. Eur. J. Biochem. 179:(2):1989;379-387.
2. Chong Y., Chen H. Preparation of functional recombinant protein from E. coli using a nondetergent sulfobetaine. Biotechniques. 6:2000;1166-1167.
3. Claret L., Hughes C. Functions of the subunits in the FlhD(2)C(2) transcriptional master regulator of bacterial flagellum biogenesis and swarming. J. Mol. Biol. 303:2000;467-478.
4. Djavadi-Ohaniance L., Friguet B., Goldberg M.E. Structural and functional influence of enzyme-antibody interactions: effects of eight different monoclonal antibodies on the enzymatic activity of E. coli tryptophan synthase. Biochemistry. 23:1984;97-104.
5. Faeder E.J., Hammes G.G. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit. Biochemistry. 9:1970;4043-4049.
6. Friguet B., Djavadi-Ohaniance L., Goldberg M.E. Polypeptide-antibody binding mechanism: conformational adaptation investigated by equilibrium and kinetic analysis. Res. Immunol. 140:1989;355-376.
7. Friguet B., Djavadi-Ohaniance L., Goldberg M.E. Immunochemical analysis of protein conformation. Creighton T.E. Protein Structure: A Practical Approach, 2nd ed., Ch 13. 1997;323-348 IRL Press, Oxford University.
8. Goldberg M.E., . Rudolph R., Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysosyme. Biochemistry. 30:1991;2790-2797.
9. Goldberg M.E., Expert-Bezançon N., Vuillard L., Rabilloud T. Non-detergent sulphobetaines: a new class of molecules that facilitate in vitro protein renaturation. Folding Des. 1:1996;21-27.
10. Groha C., Bartholmes P., Jaenicke R. Refolding and reactivation of Escherichia coli tryptophan synthase beta2 subunit after inactivation and dissociation in guanidine hydrochloride at acidic pH. Eur. J. Biochem. 92:1978;437-441.
11. Högberg-Raibaud A., Goldberg M.E. Isolation and characterization of independently folding regions of the β-chain of Escherichia coli tryptophan synthetase. Biochemistry. 16:1977;4014-4020.
12. Latta M., Knapp M., Sarmientos P., et al. Synthesis and purification of mature human serum albumin from E. coli. Biotechnology. 5:1987;1309-1314.
13. Lilie H., Schwarz E., Rudolph R. Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotechnol. 9:1998;497-501.
14. Miles E.W. The B protein of Escherichia coli tryptophan synthetase. I. Effects of sulfhydryl modification on enzymatic activities and subunit interaction. J. Biol. Chem. 245:1970;6016-6025.
15. 2 subunits are identical. Biochimie. 71:1989;533-543.
16. Ochem A.E., Skopac D., Costa M., et al. Functional properties of the separate subunits of human DNA helicase II Ku autoantigen. J. Biol. Chem. 272:1997;29919-29926.
17. Orsini G., Goldberg M.E. The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation. J. Biol. Chem. 253:1978;3453-3458.
18. Vuillard L., Braun-Breton C., Rabilloud T. Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification. Biochem. J. 305:1995;337-343.
19. Vuillard L., Rabilloud T., Goldberg M.E. Interactions of non-detergent sulfobetaines with early folding intermediates facilitate in vitro protein renaturation. Eur. J. Biochem. 256:1998;128-135.
20. 2 subunit of Escherichia coli tryptophan synthetase and its proteolytic fragments. J. Mol. Biol. 137:1980;401-414.
21. Zettlmeissl G., Rudolph R., Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry. 18:1979;5567-5571.