Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities
Résumé
Honey bee venom contains various enzymes with wide medical and pharmaceutical applications. The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee ( Apis mellifera lamarckii ) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE–cellulose and Sephacryl S-300 columns. The purified bee venom PLA2 is monomeric 16 kDa protein and has isoelectric point ( p I) of 5.9. The optimal activity of bee venom PLA2 was attained at pH 8 and 45 °C. Cu 2+ , Ni 2+ , Fe 2+ , Ca 2+ , and Co 2+ exhibited a complete activating effect on it, while Zn 2+ , Mn 2+ , NaN 3 , PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. The purified bee venom PLA2 exhibited anti-platelet aggregation and anti-coagulation activities which makes it promising agent for developing novel anti-clot formation drugs in future.
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