Chemistry of Natural Compounds

, Volume 18, Issue 1, pp 98–101 | Cite as

Transferase and hydrolase activities of phospholipase D from the roots ofAconitum arcuatum

  • Z. S. Evtushenko
  • T. V. Vlasenko
Article

Abstract

The phospholipase D fromAconitum arcuatum has been studied. The optimum pH values have been determined: 6.3 for the hydrolase activity and 8.0 for the transferase activity. Calcium ions activate the phospholipase D: the hydrolase activity most strongly at 8 and 30 µmole and the transferase activity at 30 µmole. The hydrolase activity of the phospholipase D is not activated by low concentrations of sodium dodecyl sulfate, while the transferase activity is activated to a considerable degree. The results obtained are compared with those on the activation of cabbage phospholipase D.

Keywords

Sodium Dodecyl Sulfate Lecithin Phosphatidic Acid Incubation Mixture Hydrolase Activity 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literature cited

  1. 1.
    R. H. Quarles and R. M. C. Dawson, Biochem. J.,112, 787 (1969).CrossRefGoogle Scholar
  2. 2.
    V. E. Vaskovsky, P. G. Gorovoi, and Z. S. Suppes, Int. J. Biochem.,3, 647 (1972).CrossRefGoogle Scholar
  3. 3.
    D. Nolte and L. Acker, Z. Lebensm.-Untersuch. -Forsch.,158, 149 (1975).CrossRefGoogle Scholar
  4. 4.
    S. F. Yang, S. Freer, and A. A. Benson, J. Biol. Chem.,242, 477 (1967).PubMedPubMedCentralGoogle Scholar
  5. 5.
    F. M. Davidson and C. Long, Biochem. J.,69, 458 (1958).CrossRefGoogle Scholar
  6. 6.
    M. Heller, N. Mores, J. Peri, and E. Maes, Biochim. Biophys. Acta,369, 397 (1974).CrossRefGoogle Scholar
  7. 7.
    Sh. R. Mad'yarov, Biokhimiya,41, 255 (1976).Google Scholar
  8. 8.
    S. G. Batrakov, A. G. Panosyan, G. A. Kogan, and L. D. Bergel'son, Bioorg. Khim.,1, 1593 (1975).Google Scholar
  9. 9.
    A. Joutti and O. Renkonen, Chem. Phys. Lipids,17, 264 (1969).CrossRefGoogle Scholar
  10. 10.
    R. H. Quarles and R. M. C. Dawson, Biochem. J.,112, 795 (1969).CrossRefGoogle Scholar
  11. 11.
    P. G. Roughan and C. R. Slack, Biochim. Biophys. Acta,431, 86 (1976).CrossRefGoogle Scholar
  12. 12.
    H. Brockerhoff and R. G. Jensen, Lipolytic Enzymes, Academic Press, New York (1974).CrossRefGoogle Scholar
  13. 13.
    M. Saito, E. Bourgue, and J. J. Kanfer, Arch. Biochem. Biophys.,164, 420 (1974).CrossRefGoogle Scholar
  14. 14.
    M. M. Rakhimov, Sh. R. Mad'yarov, N. R. Dzhanbaeva, and P. Kh. Yuldashev, Khim. Prir. Soedin., 738 (1970).Google Scholar
  15. 15.
    M. M. Rakhimov, Sh. R. Mad'yarov, and A. Kh. Abdumalikov, Biokhimiya,41, 452 (1976).Google Scholar
  16. 16.
    M. Heller, E. Aladyem, and B. Shapiro, Bull. Soc., Chem. Biol.,50, 1395 (1968).Google Scholar
  17. 17.
    H. Z. Stanecev, Stukhe-Sekalec, and Z. Domazet, Can. J. Biochem.,51, 747 (1973).CrossRefGoogle Scholar
  18. 18.
    M. Heller, N. Mozes, and I. Peri, Lipids,11, 604 (1976).CrossRefGoogle Scholar
  19. 19.
    A. F. Robertson and W. E. M. Lands, Biochemistry,1, 804 (1962).CrossRefGoogle Scholar

Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

  • Z. S. Evtushenko
  • T. V. Vlasenko

There are no affiliations available

Personalised recommendations