The characterization of soluble cholinesterases (ChEs) together with carboxylesterases (CEs) in as suitable biomarkers of neurotoxicity was the main aim of this study. ChEs of were characterized considering enzymatic activity, substrate affinity (acetyl-, butyryl-, propionylthiocholine), kinetic parameters ( and ) and response to model inhibitors (eserine hemisulfate, iso-OMPA, BW284C51), and carbamates (carbofuran, methomyl, aldicarb, and carbaryl). CEs were characterized based on enzymatic activity, kinetic parameters and response to carbamates (carbofuran, methomyl, aldicarb, and carbaryl). Results showed that cholinesterases from showed a substrate preference for acetylthiocholine followed by propionylthiocholine; butyrylthioline was not hydrolyzed differently from other Annelida species. CE activity was in the same range of cholinesterase activity with acetylthiocholine as substrate; the enzyme activity showed high affinity for the substrate p-nytrophenyl butyrate. Carbamates inhibited ChE activity with propionylthiocholine as substrate to a higher extent than with acetylthiocoline. Also CE activity was inhibited by all tested carbamates except carbaryl. data highlighted the presence of active forms of ChEs and CEs in that could potentially be inhibited by pesticides at environmentally relevant concentration.
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| http://dx.doi.org/10.1080/03601234.2019.1640028 | DOI Listing |
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