Abstract

BackgroundHoney bee venom contains various enzymes with wide medical and pharmaceutical applications. ResultsThe 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 (pI) of 5.9. The optimal activity of bee venom PLA2 was attained at pH 8 and 45 °C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. ConclusionsThe 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.

Highlights

  • Honey bee venom contains various enzymes with wide medical and pharmaceutical applications

  • phospholipase A2 (PLA2) can exert protective effects on airway inflammation in asthma [19]. For all these broad medical and pharmacological uses of PLA2, this study reports the isolation and biochemical characterization of PLA2 from the venom of Egyptian honey bee Apis mellifera lamarckii

  • The bee venom PLA2 was eluted from the DEAE cellulose column as one large PLA2 peak with 0.05 M NaCl and a second small PLA2 peak eluted with 0.1 M NaCl (Fig. 1a)

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Summary

Introduction

Honey bee venom contains various enzymes with wide medical and pharmaceutical applications. Apitherapy is a medication type that utilizes honey bee components like honey, pollen, royal jelly, propolis, and venom (apitoxins) to treat many human diseases. It is achieved either directly by stings of bees or indirectly through extracting the bee venom and injecting bodies with it [4]. PLA2 can exert protective effects on airway inflammation in asthma [19]. For all these broad medical and pharmacological uses of PLA2, this study reports the isolation and biochemical characterization of PLA2 from the venom of Egyptian honey bee Apis mellifera lamarckii

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