Advertisement

Enzyme pp 461-466 | Cite as

Inosine diphosphatase (nucleoside diphosphatase) from mammalian tissues

3.6.1.6 Nucleosiddiphosphate phosphohydrolase
  • Gerhard W. E. Plaut
Chapter
Part of the Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse book series (HOPPE-SEYLER)

Zusammenfassung

The discovery of this enzyme was announced almost simultaneously from several laboratories1–4. Strominger et al.1 found that a water extract of calf liver acetone powder dephosphorylated uridine triphosphate 50 times faster than adenosine triphosphate. Evidence was presented that the dephosphorylation of uridine triphosphate occurred by a series of reactions involving the enzymes adenosine triphosphate-uridine monophosphate transphorylase, nucleoside diphosphokinase, and adenosine triphosphate-adenosine monophosphate transphosphorylase, as well as a new phosphatase which hydrolyzed uridine diphosphate to uridine monophosphate and orthophosphate. Plaut2 detected a similar phosphatase in aqueous extracts of acetone desiccated mitochondria from rat liver, and of acetone powders of washed residues from beef liver. Studies with the purified enzyme from beef liver showed that inosine diphosphate is hydrolyzed to 5’-inosinic acid and orthophosnhate.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literatur

  1. 1.
    Strominger, J. L., L. A. Heppel and E. S. Maxwell: Arch. Biochem. 52, 488 (1954).CrossRefGoogle Scholar
  2. 2.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar
  3. 3.
    Gregory, J. D.: Fed. Proc. 14, 221 (1955).Google Scholar
  4. 4.
    Gibson, D. M., P. Ayengar and D. R. Sanadi: Biochim. biophys. Acta 16, 536 (1955).PubMedCrossRefGoogle Scholar
  5. 5.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959).PubMedCrossRefGoogle Scholar
  6. 6.
    Horecker, B. L., J. Hurwitz and L. A. Heppel: Am. Soc. 79, 701 (1957).CrossRefGoogle Scholar
  7. 1.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar
  8. 2.
    Strominger, J. L., L. A. Heppel and E. S. Maxwell: Arch. Biochem. 52, 488 (1954).CrossRefGoogle Scholar
  9. 3.
    Gregory, J. D.: Fed. Proc. 14, 221 (1955).Google Scholar
  10. 4.
    Gibson, D. M., P. Ayengar and D. E. Sanadi: Biochim. biophys. Acta 16, 536 (1955).PubMedCrossRefGoogle Scholar
  11. 5.
    Plaut, G. W. E.: Unpublished observations, 1955.Google Scholar
  12. 6.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959).PubMedCrossRefGoogle Scholar
  13. 7.
    Horecker, B. L.: J. biol. Ch. 183, 593 (1950).Google Scholar
  14. 1.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar
  15. 1.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959).PubMedCrossRefGoogle Scholar
  16. 1.
    Gibson, D. M., P. Ayengar and D. R. Sanadi: Biochim. biophys. Acta 16, 536 (1955).PubMedCrossRefGoogle Scholar
  17. 2.
    Fiske, C. H., and Y. Subbarow: J. biol. Ch. 66, 375 (1925).Google Scholar
  18. 3.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1967

Authors and Affiliations

  • Gerhard W. E. Plaut
    • 1
  1. 1.Laboratory for the Study of Hereditary and Metabolic Disorders and Departments of Biological Chemistry and MedicineUniversity of Utah College of MedicineSalt Lake CityUSA

Personalised recommendations