Phospholipase A
2 isozyme (PLA
2 II), which showed different mobility on native PAGE from that of the PLA
2 (PLA
2 I) purified previously, was isolated from the pyloric ceca of the starfish
Asterina pectinifera. The PLA
2 II was mainly oleic acid released from 1-palmitoyl-2-oleoyl-
sn-glycero-3-phosphocholine. The N-terminal amino acid sequence of the PLA
2 II was SVYQF. For hydrolysis of egg yolk phosphatidylcholine, the optimum pH and temperature of the PLA
2 II were at around pH 9.0 and 50°C, respectively, and the activity was enhanced by 1 mM or higher concentration of Ca
2+. The PLA
2 II as well as porcine pancreatic PLA
2 did not show fatty acid specificity for hydrolysis of phosphatidylcholine from squid mantle muscle. The PLA
2 II from the pyloric ceca of
A. pectinifera, however, hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine unlike porcine pancreatic PLA
2. These characteristics of the PLA
2 II were the same as those of the PLA
2 I.
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