Balsinde J, Mollinedo F
Centro de Investigaciones Biológicas (CSIC), Madrid, Spain.
FEBS Lett. 1990 Jan 1;259(2):237-40. doi: 10.1016/0014-5793(90)80017-d.
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.
