Contamination of commercial phosphatidylcholine by phospholipase A

During the course of a study involving the assay of a membrane-bound phospholipase A2 it was observed that a commercial preparation of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine used as substrate had intrinsic lipolytic activity at pH 8.5. Further investigation revealed a Ca2+-dependent phospholipase A largely susceptible to treatment by the alkylating reagent p-bromophenacyl bromide or by heat (15 min at 120 degrees C). Complete separation of enzyme and phospholipid could be achieved by thin-layer chromatography. Such a contamination was not observed in a chemically identical phosphatidylcholine obtained from a different supplier. These observations may be relevant to investigators using commercial preparations of phospholipids in a variety of studies, including intracellular phospholipase A2 determination.