Isolation and characteristics of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera |
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Authors: | Hideki Kishimura Kenji Hayashi |
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Affiliation: | a Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan |
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Abstract: | Phospholipase A2 was purified from the pyloric ceca of the starfish Asterina pectinifera. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 20,000. The optimum pH and temperature of the enzyme were at around pH 9.0 and 50°C, respectively, and the activity was enhanced by sodium deoxycholate and 1 mM or higher concentration of Ca2+. The enzyme had no fatty acid specificity. Starfish phospholipase A2 hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine. |
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Keywords: | Asterina pectinifera Isolation Marine invertebrate Phosphatidylcholine Phospholipase A2 Polar group specificity Pyloric cecum Starfish |
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