Skip to main content
Log in

Activation parameters and molecular changes induced by substrate hydrolysis of the adenosine triphosphatase of Micrococcus lysodeikticus. A comparison of three different soluble forms of the enzyme

  • General and Review Articles
  • a. general articles
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

The Arrhenius plots for the active and low activity soluble forms of the ATPase purified from the membranes ofMicrococcus lysodeikticus grown at 30°C presented discontinuities at 30 and 33°C, respectively. Their activation parameters differed, being highest for the low activity form of the enzyme.

Both forms underwent changes in their molecular properties as a consequence of being enzymically active, i.e., upon incubation with substrates at an adequate temperature. These changes consisted of a decrease in the relative mobilities of some of their subunits in dodecyl sulphate polyacrylamide gel electrophoresis, and the temperature at which they occurred depended on the energy of activation of the particular form of the ATPase used. The low activity form required an incubation temperature of 50°C, whereas for an active form 37°C was sufficient.

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.

Institutional subscriptions

Similar content being viewed by others

References

  1. Adolfsen, R., McClung, J. A. and Moudrianakis, E. N., 1975. Biochemistry 14, 1727–1735.

    Google Scholar 

  2. Nieto, M., Muñoz, E., Carreira, J. and Andreu, J. M., 1975. Biochim. Biophys. Acta 413, 394–414.

    Google Scholar 

  3. Carreira, J., Andreu, J. M., Nieto, M. and Muñoz, E., 1976. Molec. Cell. Biochem. 10, 67–76.

    Google Scholar 

  4. Muñoz, E., Salton, M. R. J., Ng, M. H. and Schor, M. T., 1969. Eur. J. Biochem. 7, 490–501.

    Google Scholar 

  5. Carreira, J., Muñoz, E., Andreu, J. M. and Nieto, M., 1976. Biochim. Biophys. Acta 436, 183–189.

    Google Scholar 

  6. Andreu, J. M. and Muñoz, E., 1975. Biochim. Biophys. Acta 387, 228–233.

    Google Scholar 

  7. Ayala, J. A., Nieto, M., Carreira, J. and Muñoz, E., 1976. Eur. J. Biochem. 66, 43–47.

    Google Scholar 

  8. Andreu, J. M., Albendea, J. A. and Muñoz, E., 1973. Eur. J. Biochem. 37, 505–515.

    Google Scholar 

  9. Johnson, F. H., Eyring, H. and Polissar, M. J., 1954. The Kinetic Basis of Molecular Biology p. 187, John Wiley and Sons, Inc., New York.

    Google Scholar 

  10. Dixon, M. and Webb, E. C., 1971. in Enzymes 2nd edition p. 150, Longman Group Ltd., London.

    Google Scholar 

  11. Andreu, J. M., Carreira, J. and Muñoz, E., 1976. FEBS lett. 65, 198–203.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ayala, J., Carreira, J., Nieto, M. et al. Activation parameters and molecular changes induced by substrate hydrolysis of the adenosine triphosphatase of Micrococcus lysodeikticus. A comparison of three different soluble forms of the enzyme. Mol Cell Biochem 17, 17–23 (1977). https://doi.org/10.1007/BF01732550

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01732550

Keywords

Navigation