Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities
Doaa A. Darwish, Hassan M.M. Masoud, Mohamed M. Abdel-Monsef, Mohamed S. Helmy, Hind A. Zidan, Mahmoud A. Ibrahim
Abstract
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.