Inhibition and kinetic alterations by excess free ATP and ADP of the ATP diphosphohydrolase activity (EC 3.6.1.5) from rat blood platelets

Biochem Mol Biol Int. 1995 Mar;35(3):499-506.

Abstract

ATP diphosphohydrolase (EC 3.6.1.5) catalyzes the hydrolysis of diphospho- and triphosphonucleosides and is activated by divalent cations. The enzyme described in rat blood platelets hydrolyzes Ca(2+)-ATP and Ca(2+)-ADP with a high affinity for these Ca(2+)-nucleotide complexes as substrates. In the present paper, we demonstrate that free ATP or free ADP induces inhibition and kinetic alterations of the enzyme from rat blood platelets. From these results, we draw conclusions about the binding of free nucleotides to the enzyme and their action as inhibitors with respect to calcium-nucleotide complex.

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Diphosphate / pharmacology
  • Adenosine Triphosphate / metabolism
  • Adenosine Triphosphate / pharmacology*
  • Animals
  • Apyrase / antagonists & inhibitors*
  • Apyrase / blood
  • Binding Sites
  • Blood Platelets / enzymology*
  • Calcium / metabolism
  • Cations, Divalent
  • Enzyme Activation
  • Kinetics
  • Male
  • Rats
  • Rats, Wistar
  • Substrate Specificity

Substances

  • Cations, Divalent
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Apyrase
  • Calcium