Platelet phosphorylase activity in the presence of activators and inhibitors of aggregation

Albert Deisseroth, Sidney M. Wolfe, N. Raphael Shulman

Research output: Contribution to journalArticlepeer-review

Abstract

Phosphorylase activity in suspensions of human platelets has been assayed before and after addition of thrombin and epinephrine which aggregate platelets, prostaglandins E1 and E2 and dibutyryl-3′,5′-AMP which inhibit aggregation, or sodium fluoride and isoproterenol which alter adenine nucleotide metabolism. These various reagents did not change phosphorylase a activity in intact platelets, nor did cyclic-3′,5′-AMP affect platelet phosphorylase activity in subcellular fractions. In contrast to many other tissues, platelet phosphorylase activity does not appear to be modulated by a direct effect of cyclic AMP.

Original languageEnglish (US)
Pages (from-to)551-557
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume39
Issue number3
DOIs
StatePublished - May 11 1970

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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