Resumen

GUISADO-BOURZAC, Frenkel et al. A Two-Step Purification Procedure of Phospholipases A₂ from the Sea Anemone Condylactis gigantea. Rev Cub Quim [online]. 2017, vol.29, n.1, pp. 133-149. ISSN 2224-5421.

Marine coelenterate venom is composed of complex mixtures of several substances, mainly of proteins, for which phospholipase A₂ activity has been described. This research study aims to test a two-step purification procedure for phospholipases A₂ (PLA₂) to filter enzymes for further characterization. PLA₂ purification from the sea anemone Condylactis gigantean is conducted through a chromatographic affinity support MANA-Sepharose CL 4B with covalently immobilized phosphatidylcholine egg. The phospholipase A₂ activity was corroborated by using qualitative TLC and a fluorogenic substrate. By means of the above-mentioned support, purification of three protein-based components can be carried out. These components are produced with molecular weights between 18000 and 14000, and at least one component possessing phospholipase A₂ activity.

Palabras clave : affinity; phospholipase A₂; Condylactis gigantea; sea anemone; protein purification.

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