Phospholipase A2 activity in prostasomes from human seminal plasma

Phospholipase A2 (PLA2) activity was measured and partially characterized in prostasomes isolated from human seminal plasma. The results show high PLA2 activity in seminal plasma with a threefold enrichment in the isolated prostasomes. Highest activity was found at pH 8.0 and 10.5, and there was an absolute requirement for calcium with almost total inhibition of PLA2 activity in the presence of 1 mM EDTA. Analysis with two-dimensional gel electrophoresis of prostasome material revealed a complex protein pattern with most of the proteins in the molecular weight interval of 10,000-90,000 daltons. The possible role of PLA2 in prostasomes is discussed.