Nippon Suisan Gakkaishi 67 (4), 728-734 (2001)

Partial Purification and Properties of Phospholipase A2 from the Pyloric Ceca of Starfish Coscinasterias acutispina

Noriki Koyama,1 Hideki Kishimura,1 Kenji Hayashi,1 Daisuke Fujita2

1Graduate School of Fisheries Sciences, Hokkaido University, Hokkaido 041-8611, 2Toyama Prefectural Fisheries Experimental Station, Toyama 936-8536, Japan

Phospholipase A2 (PLA2) was partially purified from the pyloric ceca of starfish Coscinasterias acutispina by gel filtration on Sephacryl S-200, DEAE-cellulose anion exchange chromatography, and gel filtration on Sephadex G-50. The final enzyme preparation was mainly released oleic acid from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The partially purified PLA2 from the pyloric ceca of C. acutispina as well as porcine pancreatic PLA2 did not show the fatty acid specificity for hydrolysis of egg yolk and soybean phosphatidylcholines. For hydrolysis of egg yolk phosphatidylcholine, the optimum pH and temperature of the partially purified PLA2 were in the range of pH10-11 and 50-60°C, respectively, and the activity was enhanced by 1mM or higher concentration of Ca2+. The partially purified PLA2 from the pyloric ceca of C. acutispina, however, hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine, unlike porcine pancreatic PLA2.


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