Isolation and characteristics of phospholipase A 2 from the pyloric ceca of the starfish Asterinapectinifera

Abstract

Phospholipase A 2 was purified from the pyloric ceca of the starfish Asterina pectinifera. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 20,000. The optimum pH and temperature of the enzyme were at around pH 9.0 and 50°C, respectively, and the activity was enhanced by sodium deoxycholate and 1 mM or higher concentration of Ca 2+. The enzyme had no fatty acid specificity. Starfish phospholipase A 2 hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine.