Partial purification and properties of phospholipase A2 from the starfish, Asterina pectinifera.
1. Phospholipase A2 (phosphatide 2-acyl-hydrolase, EC 3.1.1.4) activity was shown to occur in the supernatant fraction of a freshly prepared homogenate from the pyloric caecum of starfish (Asterina pectinifera). 2. The phospholipase A2 has been isolated and purified 130-fold by ultracentrifugation, ammonium sulfate precipitation and column chromatographic procedures. 3. The purified enzyme was stable to heat at low pH values and the optimal pH was observed at approximately 9.0. 4. The enzyme activity was activated by Ca2+ and sodium deoxycholate, and was inhibited by EDTA.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004355:Drug Stability; D004492:Edetic Acid / Q000494:pharmacology; D004589:Electrophoresis, Disc; D004789:Enzyme Activation / Q000187:drug effects; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010740:Phospholipases / Q000302:isolation & purification* / Q000378:metabolism; D011708:Pylorus / Q000201:enzymology; D013215:Starfish / Q000201:enzymology*
D003902:Detergents; D003840:Deoxycholic Acid; D004492:Edetic Acid; D010740:Phospholipases; D002118:Calcium