Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Apr;62(4):1129–1136. doi: 10.1073/pnas.62.4.1129

SOLUBILIZATION OF PARTICULATE PROTEINS AND NONELECTROLYTES BY CHAOTROPIC AGENTS*

Y Hatefi 1, W G Hanstein 1
PMCID: PMC223624  PMID: 5256411

Abstract

Chaotropic ions (those ions which favor the transfer of apolar groups to water) provide a highly effective means for the resolution of membranes and multicomponent enzymes and for increasing the water solubility of particular proteins and nonelectrolytes. The action of chaotropic agents is related to their effect on the structure and lipophilicity of water.

Full text

PDF
1129

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Castellino F. J., Barker R. The denaturing effectiveness of guanidinium, carbamoylguanidinium, and guanylguanidinium salts. Biochemistry. 1968 Nov;7(11):4135–4138. doi: 10.1021/bi00851a049. [DOI] [PubMed] [Google Scholar]
  2. Dandliker W. B., Alonso R., de Saussure V. A., Kierszenbaum F., Levison S. A., Schapiro H. C. The effect of chaotropic ions on the dissociation of antigen-antibody complexes. Biochemistry. 1967 May;6(5):1460–1467. doi: 10.1021/bi00857a031. [DOI] [PubMed] [Google Scholar]
  3. FOWLER L. R., RICHARDSON S. H., HATEFI Y. A rapid method for the preparation of highly purified cytochrome oxidase. Biochim Biophys Acta. 1962 Oct 8;64:170–173. doi: 10.1016/0006-3002(62)90770-9. [DOI] [PubMed] [Google Scholar]
  4. HOLTZER A., WANG T. Y., NOELKEN M. E. The effect of various monovalent anions on myosin B solutions. The identification of actin as a product of ATP action. Biochim Biophys Acta. 1960 Aug 26;42:453–461. doi: 10.1016/0006-3002(60)90823-4. [DOI] [PubMed] [Google Scholar]
  5. Hammes G. G., Swann J. C. Influence of denaturing agents on solvent structure. Biochemistry. 1967 Jun;6(6):1591–1596. doi: 10.1021/bi00858a004. [DOI] [PubMed] [Google Scholar]
  6. KAUZMANN W. Some factors in the interpretation of protein denaturation. Adv Protein Chem. 1959;14:1–63. doi: 10.1016/s0065-3233(08)60608-7. [DOI] [PubMed] [Google Scholar]
  7. KLEINSCHMIDT W. J., BOYER P. D. Interaction of protein antigens and antibodies. I. Inhibition studies with the egg albumin-antiegg albumin system. J Immunol. 1952 Sep;69(3):247–255. [PubMed] [Google Scholar]
  8. Klotz I. M., Farnham S. B. Stability of an amide-hydrogen bond in an apolar environment. Biochemistry. 1968 Nov;7(11):3879–3882. doi: 10.1021/bi00851a013. [DOI] [PubMed] [Google Scholar]
  9. NAGY B., JENCKS W. P. DEPOLYMERIZATION OF F-ACTIN BY CONCENTRATED SOLUTIONS OF SALTS AND DENATURING AGENTS. J Am Chem Soc. 1965 Jun 5;87:2480–2488. doi: 10.1021/ja01089a030. [DOI] [PubMed] [Google Scholar]
  10. Packer L., Deamer D. W., Heath R. L. Regulation and deterioration of structure in membranes. Adv Gerontol Res. 1967;2:77–120. [PubMed] [Google Scholar]
  11. ROBINSON D. R., JENCKS W. P. THE EFFECT OF CONCENTRATED SALT SOLUTIONS ON THE ACTIVITY COEFFICIENT OF ACETYLTETRAGLYCINE ETHYL ESTER. J Am Chem Soc. 1965 Jun 5;87:2470–2479. doi: 10.1021/ja01089a029. [DOI] [PubMed] [Google Scholar]
  12. Rieske J. S., Baum H., Stoner C. D., Lipton S. H. On the antimycin-sensitive cleavage of complex 3 of the mitochondrial respiratory chain. J Biol Chem. 1967 Nov 10;242(21):4854–4866. [PubMed] [Google Scholar]
  13. VONHIPPEL P. H., WONG K. Y. NEUTRAL SALTS: THE GENERALITY OF THEIR EFFECTS ON THE STABILITY OF MACROMOLECULAR CONFORMATIONS. Science. 1964 Aug 7;145(3632):577–580. doi: 10.1126/science.145.3632.577. [DOI] [PubMed] [Google Scholar]
  14. WOLFF J. The effect of thyroxine on isolated dehydrogenases. II. Sedimentation changes in glutamic dehydrogenase. J Biol Chem. 1962 Jan;237:230–235. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES