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Although apparent phospholipase A2 activity is very low in freshly prepared hepatopancreas homogenates of red sea bream, its activity increased considerably during autolysis.Hence, phospholipase A2 was purified about 14,500-fold from the dialyzate of delipidated powder of frozen hepatopancreas homogenate by the sequential use of column chromatographies on DEAE-sepharose CL-6B, Toyopearl HW-55F, reversed phase HPLC, and TSK-GEL G3000SW.The final enzyme preparation was nearly homogeneous in SDS-polyacrylamide gel electrophoresis, and its molecular weight was estimated to be approximately 20,000. Purified enzyme had a pH optimum of 8.0 for phosphatidylethanolamine and essentially required Ca2+ for activity. These properties of red sea bream hepatopancreas phospholipase A2 were similar to those of the secretory enzymes of mammalian pancreatic or snake venom phospholipase A2.

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