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Updated: Jun 12, 2026

Identification of Hemolytic and Phospholipase Activity in Crude Extracts from Sea Anemones by Straightforward Bioassays
Published on: March 29, 2022
Enzymatic and structural characterization of a basic phospholipase A(2) from the sea anemone Condylactis gigantea
Lazara Romero1, Silvana Marcussi, Daniela P Marchi-Salvador
1Centro de Estudios de Proteínas, Facultad de Biología, Universidad de La Habana, Cuba.
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 pI 8.6 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(2)s from Adamsia carciniopados, Nematostella vectensis, Vipera russelli russelli and Bothrops jararacussu, respectively.
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