Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii

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Apyrase is one of the essential platelet aggregation inhibitors in hematophagous arthropods due to its ability to hydrolyze ATP and ADP molecules. Here, an apyrase (TNapyrase) with antiplatelet aggregation activity was purified and characterized from the nymphs of the camel tick Hyalomma dromedarii through anion exchange and gel filtration columns. The homogeneity of TNapyrase was confirmed by native-PAGE, SDS-PAGE as well as with isoelectric focusing. Purified TNapyrase had a molecular mass of 25 kDa and a monomer structure. TNapyrase hydrolyzed various nucleotides in the order of ATP > PPi > ADP > UDP > 6GP. The Km value was 1.25 mM ATP and its optimum activity reached at pH 8.4. The influence of various ions on TNapyrase activity showed that FeCl2, FeCl3 and ZnCl2 are activators of TNapyrase. EDTA inhibited TNapyrase activity competitively with a single binding site on the molecule and Ki value of 2 mM. Finally, TNapyrase caused 70% inhibition of ADP-stimulated platelets aggregation and is a possible target for antibodies in future tick vaccine studies.

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Adenosine diphosphates


Adenosine triphosphates




Inorganic phosphate


Platelet poor plasma


Platelet rich plasma


Tick nymph apyrase


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The National Research Centre, Egypt is greatly appreciated for funding this study.

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Correspondence to Hassan M. M. Masoud.

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Masoud, H.M.M., Helmy, M.S., Darwish, D.A. et al. Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii. Exp Appl Acarol (2020) doi:10.1007/s10493-020-00471-9

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  • Camel tick nymph
  • Hyalomma dromedarii
  • Apyrase
  • Purification
  • Antiplatelet aggregation