Abstract
An intracellular form of phospholipase A 2 was purified about 47,500-fold to near homogeneity from bovine platelets 100,000 × g supernatant by sequential use of column chromatographies on Heparin-Sepharose, DEAE-Sephacel, Butyl-Toyopearl, Sephacryl S-300, DEAE-5PW HPLC, TSK G 3000 SW HPLC and Mono Q FPLC. The final preparation showed a single band on SDS-polyacrylamide gel, and its molecular mass was estimated to be approximately 100,000 daltons. The purified PLA 2 showed maximal activity at alkaline pH(pH 9.0–10.0) and considerable activity at 0.3–1.0μM calcium concentration. It hydrolyzed phosphatidylcholine containing arachidonate at sn-2 position with high selectivity in comparison to linoleate.
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