Advertisement

Experientia

, Volume 27, Issue 6, pp 633–635 | Cite as

The effect of pyruvate on cyanide-inhibited respiration in intact ascites tumor cells

  • A. Cittadini
  • T. Galeotti
  • T. Terranova
Specialia Chimica, Biochimica, Biophysica

Keywords

Pyruvate Cyanide Amyotrophic Lateral Sclerosis Rotenone Cytochrome Oxidase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Riassunto

È stato osservato che l'aggiunta di piruvato a cellule ascite di Ehrlich del topo è capace di rimuovere rapidamente l'inibizione della respirazione indotta da cianuro, restaurando l'integrità della fosforilazione ossidativa.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literatur

  1. 1.
    O. Warburg,Heavy Metal Prosthetic Groups and Enzyme Action (Oxford University Press, London 1949).Google Scholar
  2. 2.
    E. C. Slater, Biochem. J.46, 484 (1950).CrossRefPubMedPubMedCentralGoogle Scholar
  3. 3.
    C. L. Tsou, Biochem. J.49, 512 (1951).CrossRefPubMedPubMedCentralGoogle Scholar
  4. 4.
    D. Keilin andT. E. King, Proc. R. Soc., Lond. Ser. B152, 163 (1960).CrossRefGoogle Scholar
  5. 5.
    M. Dixon andE. C. Webb,Enzymes (Academic Press, New York 1964), p. 317.Google Scholar
  6. 6.
    P. W. Camerino andT. E. King, J. biol. Chem.241, 970 (1966).PubMedGoogle Scholar
  7. 7.
    H. A. Krebs, quoted byO. Warburg (ref. 1 ).Google Scholar
  8. 8.
    H. Wieland andA. Bertho, Justus Liebigs Annln Chem.467, 95 (1928).CrossRefGoogle Scholar
  9. 9.
    B. Kisch, Biochem. Z.263, 75 (1933).Google Scholar
  10. 10.
    D. E. Green andS. Williamson, Biochem. J.31, 617 (1936).CrossRefGoogle Scholar
  11. 11.
    B. Chance andB. Hagihara, Proc. Fifth Internat. Congr. of Biochemistry, Moscow, 1961 (Ed.A. N. M. Sissakian; Pergamon Press, New York 1963), vol. 5, p. 3.Google Scholar
  12. 12.
    B. Chance andB. Hess, J. biol. Chem.234, 2404 (1959).PubMedGoogle Scholar
  13. 13.
    C. P. Lee, K. Nordenbrand andL. Ernster, inOxidases and Related Redox Systems (Eds.T. E. King, H. S. Mason andM. Morrison; John Wiley, New York 1965), p. 960.Google Scholar
  14. 14.
    L. Packer andM. G. Mustafa, Biochim. biophys. Acta113, 1 (1966).CrossRefPubMedGoogle Scholar
  15. 15.
    T. Terranova, T. Galeotti, S. Baldi andG. Neri, Biochem. Z.346, 439 (1967).PubMedGoogle Scholar
  16. 16.
    G. Dallner andL. Ernster, Expl. Cell Res.27, 372 (1962).CrossRefGoogle Scholar
  17. 17.
    O. Dionisi, A. Cittadini, G. Gelmuzzi, T. Galeotti andT. Terranova, Biochim. biophys. Acta216, 71 (1970).CrossRefPubMedGoogle Scholar
  18. 18.
    R. B. Beechey, Biochem. J.98, 284 (1966).CrossRefPubMedPubMedCentralGoogle Scholar
  19. 19.
    B. Chance andG. R. Williams, J. biol. Chem.217, 409 (1955).PubMedGoogle Scholar
  20. 20.
    B. Chance, Rev. scient. Instrum.22, 634 (1951).CrossRefGoogle Scholar

Copyright information

© Birkhäuser Verlag 1971

Authors and Affiliations

  • A. Cittadini
    • 1
  • T. Galeotti
    • 1
  • T. Terranova
    • 1
  1. 1.Institute of General PathologyCatholic University, Via Pineta Sacchetti 644RomaItaly

Personalised recommendations