Partial purification and characteristics of phospholipase A2 from pyloric ceca of starfish Plazaster borealis

Phospholipase A activities in the pyloric ceca and viscera from six species of marine invertebrates were determined. A high activity of the enzyme was found in the pyloric ceca of the starfish Plazaster borealis. Phospholipase A2 was partialy purified from the pyloric ceca of the P. borealis. The enzyme was purified 12-fold from the crude enzyme solution with a yield of 5 %. The optimum pH and temperature of the enzyme were approximately 10.0 and 50T, respectively, and the activity was enhanced by Ca2+ at I mM or higher. The enzyme had no fatty acid specificity. Partialy purified P. borealis phospholipase A2 hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine similar to other starfish phospholipase A 2 •