Non-detergent sulphobetaines: A new class of molecules that facilitate in vitro protein renaturation

Folding and Design

Volumn 1, Issue 1, 1996, Pages 21-27

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

^a INSTITUT PASTEUR   (France)

^b INSTITUT LAUE LANGEVIN   (France)

^c CEA GRENOBLE   (France)

Author keywords

Aggregation; Protein folding; Renaturation; Sulphobetaines

Indexed keywords

BETA GALACTOSIDASE; BETAINE; DRUG DERIVATIVE; LYSOZYME;

ANIMAL; ARTICLE; CHEMISTRY; CHICKEN; ENZYMOLOGY; ESCHERICHIA COLI; FEMALE; IN VITRO STUDY; PROTEIN FOLDING;

ANIMALS; BETA-GALACTOSIDASE; BETAINE; CHICKENS; ESCHERICHIA COLI; FEMALE; MURAMIDASE; PROTEIN FOLDING;

EID: 0030347883     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00008-9     Document Type: Article

References (26)

1. Thatcher, D.R. & Hitchcock, A. (1994). Protein folding in biotechnology. In Mechanisms of Protein Folding. (R. Pain, ed.), pp 229-261, Oxford University Press, Oxford.
2. Orsini, G. & Goldberg, M.E. (1978). The renaturation of reduced chymotrypsinogen A in guanidine-HCl; refolding versus aggregation. J. Biol. Chem. 253, 3453-3458.
3. Zettlmeissl, G., Rudolph, R. & Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1-Physical properties and kinetics of aggregation. Biochemistry 18, 5567-5571.
4. Kiefhaber, T., Rudolph, R., Kohler, H.H. & Buchner, J. (1991). Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology 9, 825-829.
5. Goloubinoff, P., Gattenby, A.A. & Lorimer, G. (1989). Gro E heat-shock proteins promote assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli. Nature 337, 44-47.
6. Buchner, J., et al. & Kiefhaber, T. (1991). Gro E facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
7. Ellis, J. & Van de Vries, S.M. (1991). Molecular chaperones. Annu. Rev. Biochem. 60, 321-347.
8. Hartl, F.-U., Martin, J. & Neupert, W. (1992). Protein folding in the cell: the role of molecular chaperones Hsp 70 and Hsp 60. Annu. Rev. Biophys. Biomol. Struct. 21, 293-322.
9. Winkler, M.E. & Blaber, M. (1986). Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli. Biochemistry 25, 4041-4045.
10. Cleland, J.L. & Wang, D.I.C. (1990). Cosolvent assisted protein folding. Biotechnology 8, 1274-1278.
11. Zardeneta, G. & Horowitz, P.M. (1992). Micelle-assisted protein folding: denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation. J. Biol. Chem. 267, 5811-5816.
12. Rozema, D. & Gellman S.H. (1995). Artificial chaperones: protein refolding via sequential use of detergent and cyclodextrin. J. Am. Chem. Soc. 117, 2373-2374.
13. Vuillard, L., Rabilloud, T., Leberman, R., Berthet, C. & Cusak, S. (1994). A new additive for protein crystallization. FEBS Lett. 353, 294-296.
14. Vuillard, L., Braun-Breton, C. & Rabilloud, T. (1995). Non-detergent sulphobetaines: a new class of mild solubilizing agents for protein purification. Biochem. J. 305, 337-343.
15. Vuillard, L., Madern, D., Franzetti, B. & Rabilloud, T. (1995). Halophilic protein stabilization by the mild solubilization agents nondetergent sulphobetaines. Analyt. Biochem. in press.
16. Jacobson, R.H., Zhang, X.-J., DuBose, R.F. & Matthews, B.W. (1994). Three-dimensional structure of β-galactosidase from E. coli. Nature 369, 761-766.
17. Goldberg, M.E., Rudolph, R. & Jaenicke, R. (1991). A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30, 2790-2797.
18. Perrin, D. & Monod, J. (1963). On the reversibility by treatment with urea of the thermal inactivation of Escherichia coli β-galactosidase. Biochem. Biophys. Res. Com. 12, 425-428.
19. Ullmann, A. & Monod, J. (1969). On the effect of divalent cations and protein concentration upon renaturation of β-galactosidase from Escherichia coli. Biochem. Biophys. Res. Com. 35, 35-42.
20. Goldberg, M.E. & Guillou, Y. (1994). Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme. Prof. Sci. 3, 883-887.
21. Dobson, C.M., Evans, P.A., & Radford, S.E. (1994). Understanding how proteins fold: the lysozyme story so far. Trends Biochem Sci 19, 31-37.
22. Goldberg, M.E. (1969). Tertiary structure of Escherichia coli β-D-galactosidase. J. Mol. Biol. 46, 441-446.
23. Goldberg, M.E. (1970). Structural studies of φ-complemented β-galactosidase of Escherichia coli. In The Lactose Operon. (Beckwith, J. & Zipser, D., eds.), pp 273-278, Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
24. Ullmann, A., Jacob, F. & Monod, J. (1968). On the subunit structure of wild-type and complemented β-galactosidase of Escherichia coli. J. Mol. Biol. 32, 1-13.
25. Wettlaufer, D.B., Johnson, E.R. & Clauss, LM. (1974). Rapid nonenzymic regeneration of reduced human leukemia lysozyme. In Lysozyme. (Osserman, E.F., Canfield, R.E. & Beychok, S., eds.), pp 269-280, Academic Press, New York and London.
26. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.