Skip to main content

Advertisement

Log in

Thermodynamic Aspects of the Action of Phosphohexoseisomerase

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

THE isomerization of glucose-6-phosphate⇄fructose-6-phosphate is catalysed by the enzyme phosphohexoseisomerase1, and at equilibrium a mixture of aldose and ketose in the proportion of 6/4 is present2,3. Although Bruns and Hinsberg2 have investigated the kinetics of this isomerase system by the method which was also employed in the present experiments, the thermodynamic properties of this reaction have not been studied.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Lohmann, K., Biochem. Z., 262, 137 (1933).

    CAS  Google Scholar 

  2. Bruns, F., and Hinsberg, K., Biochem. Z., 325, 532 (1954).

    CAS  PubMed  Google Scholar 

  3. Bodansky, O., J. Biol. Chem., 202, 829 (1953).

    CAS  PubMed  Google Scholar 

  4. Lewis, G. N., and Randall, M., “Thermodynamics”, 264 (McGraw-Hill Book Co., Inc., New York, 1923).

    Google Scholar 

  5. Glasstone, S., Laidler, K. J., and Eyring, H., “The Theory of Rate Process” (McGraw-Hill Book Co., Inc., New York, 1948).

    Google Scholar 

  6. Pauling, L., “Nature of the Chemical Bond” (Cornell Univ. Press, Ithaca, New York, 1948). Pitzer, K. S., “Quantum Chemistry”, 170 (Prentice-Hall Inc., New York, 1953).

    Google Scholar 

  7. Stearn, A. E., “Advances in Enzymology”, 9, 25 (1949).

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

BRUNS, F., OKADA, S. Thermodynamic Aspects of the Action of Phosphohexoseisomerase. Nature 177, 87–88 (1956). https://doi.org/10.1038/177087a0

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/177087a0

  • Springer Nature Limited

This article is cited by

Navigation