Molecular and Cellular Biochemistry

, Volume 129, Issue 1, pp 47–55 | Cite as

Characterization of an ATP diphosphohydrolase activity (APYRASE, EC 3.6.1.5) in rat blood platelets

  • Silvana S. Frassetto
  • Renato D. Dias
  • João J. F. Sarkis
Article
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Accepted:

Abstract

In the present report we describe an apyrase (ATP diphosphohydrolase, EC 3.6.1.5) in rat blood platelets. The enzyme hydrolyses almost identically quite different nucleoside di- and triphosphates. The calcium dependence and pH requirement were the same for the hydrolysis of ATP and ADP and the apparent Km values were similar for both Ca2+-ATP and Ca2+-ADP as substrates. Ca2+-ATP and Ca2+-ADP hydrolysis could not be attributed to the combined action of different enzymes because adenylate kinase, inorganic pyrophosphatase and nonspecific phosphatases were not detected under our assay conditions. The Ca2+-ATPase and Ca2+-ADPase activity was insensitive to ATPase, adenylate kinase and alkaline phosphatase classical inhibitors, thus excluding these enzymes as contaminants. The results demonstrate that rat blood platelets contain an ATP diphosphohydrolase involved in the hydrolysis of ATP and ADP which are vasoactive and platelet active adenine nucleotides.

Key words

ATP diphosphohydrolase apyrase platelets rat blood 
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Copyright information

© Kluwer Academic Publishers 1993

Authors and Affiliations

  • Silvana S. Frassetto
    • 1
  • Renato D. Dias
    • 1
  • João J. F. Sarkis
    • 1
  1. 1.Instituto de Biociências, Departamento de BioquímicaUniversidade Federal do Rio Grande do SulPorto AlegreBrasil

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