ニチリンヒトデ幽門盲のうホスホリパーゼA_2様酵素の精製と性質 Purification and Properties of Phospholipase A_2-like Enzyme from the Pyloric Caeca of the Starfish Solaster Paxillatus
Phospholipase A<sub>2</sub>-like enzyme was purified from the crude extracts of the pyloric caeca of the starfish <i>Solaster paxillatus</i> by heat treatment followed by gel filtration on a Sephacryl S-200, preparative polyacrylamide gel electrophoresis, and gel filtration on a Sephadex G-50.<br>The final phospholipase A<sub>2</sub>-1ike enzyme preparation was nearly homogeneous in SDS-polyacrylamide gel electrophoresis, and its molecular weight was estimated to be approximately 13, 000. The enzyme mainly released oleic acid from 1-palmitoyl-2-o1eoy1-<i>sn</i>-glycero-3-phosphocholine. For hydrolysis of egg yolk phosphatidylcho1ine, the optimum pH and temperature of this enzyme were in the range of pH 9-10 and 30-40°C, respectively, and the enzyme was activated by Ca<sup>2+</sup>. Starfish phospholipase A<sub>2</sub>-1ike enzyme as well as porcine pancreatic phospholipase A<sub>2</sub> did not show the fatty acid specificity for hydrolysis of phosphatidylcholine prepared from scallop adductor muscle.
日本水産学会誌 64(2), 264-269, 1998-03-15