Protein kinase C from rat brain and human neutrophils was chromatographically separated on a hydroxylapatite column connected to a high-performance liquid chromatography (HPLC) system. Protein kinase C from rat brain was separated into three peaks (types I, II, and III). In contrast, only two types were obtained from human neutrophils matching type II and type III in brain. In cell membranes from unstimulated human neutrophils type III was predominant, but mainly type II was translocated to the membranes upon stimulation with phorbolmyristatacetate (PMA). Both types were equivalently activated by phosphatidylserine, diolein, and magnium and presented identical Km for ATP.
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