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 language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - May 11 1970|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology