Experientia

, Volume 40, Issue 3, pp 259–261 | Cite as

Regulatory properties of 14-day embryo and adult hen heart AMP-deaminase; the influence of pH on the enzyme activity

  • K. Kaletha
Short Communications

Summary

The variation of kinetic parameters with pH for the reaction catalysed by the purified 14-day embryo and adult hen heart AMP-deaminase was shown to be similar but not identical. The pH-dependence of the half-saturation constant (K0.5) is well pronounced, and the plot of pK0.5 vs pH is manifested as a bell-shaped curve for both developmental forms of the enzyme. In contrast to that, the maximum velocity of the reaction (Vmax) catalyzed by these enzymes does not change significantly in the range pH 5.6–7.4.

Keywords

Enzyme Enzyme Activity Kinetic Parameter Maximum Velocity Regulatory Property 

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References

  1. 2.
    Purzycka-Preis, J., Prus, E., Wożniak, M., and Żydowo, M>, Biochem. J.175 (1978) 607.PubMedGoogle Scholar
  2. 3.
    Kaletha, K., and Skladanowski, A., Biochim. biophys. Acta568 (1979) 80.PubMedGoogle Scholar
  3. 4.
    Barsacchi, R., Rainieri-Raggi, M., Bergamini, C., and Raggi, A., Biochem. J.182 (1979) 361.PubMedGoogle Scholar
  4. 5.
    Kaletha, K., Skladanowski, A., Bogdanowicz, S., and Żydowo, M., Int. J. Biochem.10 (1979) 925.CrossRefPubMedGoogle Scholar
  5. 6.
    Skladanowski, A., Kaletha, K., and Żydowo, M., Int. J. Biochem.9 (1978) 43.CrossRefPubMedGoogle Scholar
  6. 7.
    Kaletha, K., Int. J. Biochem., in press.Google Scholar
  7. 8.
    Kaletha, K., and Skladanowski, A., Experientia37 (1981) 232.PubMedGoogle Scholar
  8. 9.
    Kaletha, K., and Skladanowski, A., Int. J. Biochem., in press.Google Scholar
  9. 10.
    Smiley, K.L., Berry, A., and Suelter, C.H., J. biol. Chem.242 (1967) 2502.PubMedGoogle Scholar
  10. 11.
    Chaney, A.L., and Marbach, E.P., Clin. Chem.8 (1962) 130.Google Scholar
  11. 12.
    Wilkinson, G.N., Biochem. J.80 (1961) 324.PubMedGoogle Scholar
  12. 13.
    Dixon, M., and Webb, E.C., in: Enzymes, pp. 128 and 137. Longman, London 1971.Google Scholar
  13. 14.
    Bohnensack, R., and Hofmann, E., Acta biol. med. germ.24 (1970) 765.PubMedGoogle Scholar
  14. 15.
    Dixon, M., Biochem. J.55 (1953) 61.Google Scholar
  15. 16.
    Parkash, D., and Bhatia, I.S., Biochem. J.185 (1980) 609.PubMedGoogle Scholar
  16. 17.
    Fromm, H.J., Initial Rate Enzyme Kinetics, p. 204. Springer, Berlin-Heidelberg-New York 1975.Google Scholar

Copyright information

© Birkhäuser Verlag 1984

Authors and Affiliations

  • K. Kaletha
    • 1
  1. 1.Department of BiochemistryMedical SchoolGdansk(Poland)

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