Abstract
The denaturation of proteins by guanidine hydrochloride was studied in the presence of different concentrations of stabilizing salts, namely potassium phosphate, ammonium sulfate, and potassium acetate. The denaturation transition was followed by observing changes in the peptide circular dichroism atpH 7.0 and 25°C. From these results the free energy of stabilization for the process native ⇄ denatured was determined. It was found that the stabilizing power of the anions increased in the order acetate < sulfate < phosphate, in agreement with the anionic lyotropic series. Ribonuclease A, which is known to have a site that can bind either a phosphate or a sulfate ion, showed a larger stabilization by these anions than that for lysozyme, pepsinogen, and myoglobin.
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References
Ahmad, F. (1984).J. Biol. Chem. 259, 4183–4186.
Ahmad, F., and Bigelow, C. C. (1982).J. Biol. Chem. 247, 12935–12938.
Ahmad, F., and McPhie, P. (1978).Biochemistry 17, 241–246.
Ahmad, F., and Salahuddin, A. (1974).Biochemistry 13, 245–249.
Anderson, D. G., Hammes, G. G., and Walz, Jr., F. G. (1968).Biochemistry 7, 1637–1645.
Arakawa, T., and Timasheff, S. N. (1985).Meth. Enzymol. 117, 60–65.
Arnon, R., and Perlmann, G. E. (1963).J. Biol. Chem. 238, 963–968.
Barnard, E. A. (1964).J. Mol. Biol. 10, 235–262.
Bigelow, C. C. (1960).C.R. Trav. Lab. Carlsberg 31, 305–324.
Bigelow, C. C. (1964).J. Mol. Biol. 8, 696–700.
Bull, H. B., and Breese, K. (1970).Arch. Biochem. Biophys. 137, 299–305.
Edelhoch, H., and Osborn, Jr., J. C. (1976).Adv. Protein Chem. 30, 183–250.
Ginsburg, A., and Carroll, W. R. (1965).Biochemistry 4, 2159–2174.
Hamaguchi, K., and Kurono, A. (1963).J. Biochem. (Tokyo)54, 111–122.
Hofmeister, F. (1888).Arch. Exp. Pathol. Pharmokol. 24, 247–262.
McPhie, P. (1972).Biochemistry 11, 879–883.
Melander, W., and Horvath, C. (1977).Arch. Biochem. Biophys. 183, 200–215.
Nelson, C. A., and Hummel, J. P. (1961).J. Biol. Chem. 236, 3173–3176.
Nelson, C. A., Hummel, J. P., Swenson, C. A., and Friedman, L. (1962).J. Biol. Chem. 237, 1575–1580.
Nozaki, Y. (1972).Meth. Enzymol. 26, 43–50.
Pace, C. N. (1975).CRC Crit. Rev. Biochem. 3, 1–43.
Puett, D. (1973).J. Biol. Chem. 248, 4623–4634.
Record, Jr., M. T., Anderson, C. F., and Lohman, T. M. (1978).Q. Rev. Biophys. 12, 103–178.
Richards, F. M., and Wyckoff, H. W. (1971). InThe Enzymes, Vol. 4, pp. 647–806.
Saito, Y., and Wada, A. (1983).Biopolymers 22, 2105–2132.
Schellman, J. A., and Hawkes, R. B. (1980). InProtein Folding (Jaenike, R., ed.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 331–341.
Sela, M., Anfinsen, C. B., and Harrington, W. F. (1957).Biochim. Biophys. Acta 26, 502–512.
Tanford, C. (1961).Physical Chemistry of Macromolecules, Wiley, New York.
Tanford, C. (1968).Adv. Protein Chem. 23, 121–282.
Tanford, C. (1972). InPolymerization in Biological Systems, Ciba Foundation Symposium 7, ASP, Amsterdam, pp. 125–146.
Thomson, J. A., and Bigelow, C. C. (1986).Biochem. Cell Biol., in press.
Von Hippel, P. H., and Schleich, T. (1969). InStructure and Stability of Macromolecules (Timasheff, S. N., and Fasman, G. D., eds.), Marcel Dekker, New York, Vol. 2, pp. 417–574.
Von Hippel, P. H., and Wong, K.-Y. (1964).Science 145, 577–580.
Von Hippel, P. H., and Wong, K.-Y. (1965).J. Biol. Chem. 240, 3909–3923.
Wolf, A. V., Brown, M. G., and Prentiss, P. G. (1975/1976). InHandbook of Chemistry and Physics (Weast, R. C., ed.), CRC Press, pp. D-218-267.
Wyman, J. (1964).Adv. Protein Chem. 19, 223–286.
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Ahmad, F., Bigelow, C.C. Thermodynamic stability of proteins in salt solutions: A comparison of the effectiveness of protein stabilizers. J Protein Chem 5, 355–367 (1986). https://doi.org/10.1007/BF01025963
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DOI: https://doi.org/10.1007/BF01025963