ArticleExperimental & applied acarology2020
Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii.
Article in Experimental & applied acarology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Potential mechanisms implied in tick infection by arboviruses and their transmission to vertebrate hosts.Integrative zoology · 2025Review
- Genome-Wide Investigation of Apyrase (APY) Genes in Peanut (International journal of molecular sciences · 2023Article
- Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks.Parasites & vectors · 2021Article
- RNA-seq analysis and gene expression dynamics in the salivary glands of the argasid tick Ornithodoros erraticus along the trophogonic cycle.Parasites & vectors · 2021Article
- Sialotranscriptomics of the argasid tick Ornithodoros moubata along the trophogonic cycle.PLoS neglected tropical diseases · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 K
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