Disulfide pairings and active site residues are highly conserved in secretory phospholipases A2 (PLA2s). However, secretory PLA2 s of marine inverte-brates display some distinctive structural features. In this study, we report the isolation and characterization of a PLA2 from the northern Pacific sea anemone,Urticina crassicornis(UcPLA2), containing a C27N substitution and a truncated C-terminal Tom Turk1 1 2 3 4 Biotechnical Faculty, Department of Biology, University of Ljubljana, Slovenia ˇ Department of Molecular and Biomedical Sciences, Jozef Stefan Institute, Ljubljana, Slovenia Faculty of Veterinary Medicine, University of Ljubljana, Slovenia Department of Pharmacology and Therapeutics, College of Medicine, University of Florida, Gainesville, FL, USA Keywords enzymatic activity; phospholipase.
