The presence of diadenosine 5',5'''-P1,P3-triphosphate (Ap3A) in human platelets

Biochem Biophys Res Commun. 1983 Aug 30;115(1):253-60. doi: 10.1016/0006-291x(83)90997-x.

Abstract

Diadenosine triphosphate (Ap3A) has been identified and quantified in human platelets using a coupled enzymatic assay specific for Ap3A, after fractionation of acidic extracts with high-performance liquid chromatography. Upon thrombin-induced aggregation, Ap3A is released together with the homologue diadenosine tetraphosphate (Ap4A). Extracts of human platelets do also contain enzymatic activities that degrade diadenosine tetraphosphate as well as diadenosine triphosphate. These enzymes, however, are not released during thrombin-induced aggregation of the platelets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases*
  • Adenine Nucleotides / blood*
  • Adenine Nucleotides / isolation & purification
  • Blood Platelets / metabolism*
  • Chromatography, High Pressure Liquid
  • Dinucleoside Phosphates*
  • Humans
  • Hydrolysis
  • Kinetics
  • Neoplasm Proteins*
  • Phosphoric Diester Hydrolases / blood

Substances

  • Adenine Nucleotides
  • Dinucleoside Phosphates
  • Neoplasm Proteins
  • fragile histidine triad protein
  • diadenosine tetraphosphate
  • diadenosine triphosphate
  • Phosphoric Diester Hydrolases
  • Acid Anhydride Hydrolases