Abstract
The [32P]PIP2/[32P]PA and the [32P]PIP/[32P]PA relationships were demonstrated to be remarkably similar after stimulation of [32P]Pi-prelabelled platelets for 90 s with various combinations and concentrations of agonists and inhibitors. Thus the activity of the PI and PIP kinases with the corresponding phosphomonoesterases may be tightly controlled during receptor-mediated platelet stimulation involving phospholipase C activation.