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Enzymatic and structural characterization of a basic phospholipase A <inf>2</inf> from the sea anemone Condylactis gigantea

Abstract:

This work aimed at the isolation and structural/functional characterization of a phospholipase A 2 (CgPLA 2) from the extract of the anemone Condylactis gigantea. CgPLA 2 was isolated with a high purity level through three chromatographic steps, showing pIΓ8.6 and molecular weights of 14,500 and 29,000 for the monomer and dimer, respectively. CgPLA 2 showed a high catalytic activity upon fluorescent phospholipids inducing no direct hemolytic activity. This enzyme, which is Ca 2+-dependent, showed a lower stability against temperature and pH variations when compared with snake venom enzymes. The enzymatic activity was significantly reduced or completely abolished after chemical modification of CgPLA 2 with BPB. Its cDNA was then obtained, with 357 base pairs which codified for a mature protein of 119 amino acid residues. A comparative analysis of the primary structure of CgPLA 2 revealed 84%, 61%, 43% and 42% similarity to the PLA 2s from Adamsia carciniopados, Nematostella vectensis, Vipera russelli russelli and Bothrops jararacussu, respectively. © 2010 Elsevier Masson SAS.