ニチリンヒトデ幽門盲のうホスホリパーゼA2様酵素の精製と性質
1998 年 64 巻 2 号 p. 264-269
詳細
1998 年 64 巻 2 号 p. 264-269
Phospholipase A2-like enzyme was purified from the crude extracts of the pyloric caeca of the starfish Solaster paxillatus by heat treatment followed by gel filtration on a Sephacryl S-200, preparative polyacrylamide gel electrophoresis, and gel filtration on a Sephadex G-50.
The final phospholipase A2-1ike 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-sn-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 Ca2+. Starfish phospholipase A2-1ike enzyme as well as porcine pancreatic phospholipase A2 did not show the fatty acid specificity for hydrolysis of phosphatidylcholine prepared from scallop adductor muscle.
