A phospholipase D activity able to hydrolyze phosphatidylinositol has previously been described in the cytosol of human neutrophils. The experiments reported here demonstrate that this phosphatidylinositol-hydrolyzing phospholipase D activity is also present in human plasma. This activity was assessed by free inositol release from phosphatidylinositol substrate, by phosphatidate formation and by phosphatidylethanol formation through its capacity of catalyzing a transphosphatidylation reaction. This plasma enzyme activity shows an optimum pH of 8.0 and is inhibited by EGTA.
