Partial purification and properties of phospholipase A2 from the pyloric ceca of starfish Coscinasterias acutispina

Phospholipase A(2) (PLA(2)) was partially purified from the pyloric ceca of starfish Coscinasterias acutispina by gel filtration on Sephacryl S-200, DEAF-cellulose anion exchange chromatography, and gel filtration on Sephadex G-50. The final enzyme preparation was mainly released oleic acid from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The partially purified PLA(2) from the pyloric ceca of C. acutispina as well as porcine pancreatic PLA(2) did not show the fatty acid specificity for hydrolysis of egg yolk and soybean phosphatidylcholines. For hydrolysis of egg yolk phosphatidylcholine, the optimum pH and temperature of the partially purified PLA(2) were in the range of pH 10-11 and 50-60 degreesC, respectively, and the activity was enhanced by I mM or higher concentration of Ca2+. The partially purified PLA(2) from the pyloric ceca of C. acutispina, however, hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine, unlike porcine pancreatic PLA(2).