ArticleEcotoxicology (London, England)2007
Malathion, carbofuran and paraquat inhibit Bungarus sindanus (krait) venom acetylcholinesterase and human serum butyrylcholinesterase in vitro.
Article in Ecotoxicology (London, England), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 41 citations in OpenAlex.
- Acetylcholinesterase and butyrylcholinesterase co-immobilized on a copper containing Prussian blue modified electrode for the broad screening of insecticides.Analytical and bioanalytical chemistry · 2024Article
- Isolation and Identification of Efficient Malathion-Degrading Bacteria from Deep-Sea Hydrothermal Sediment.Microorganisms · 2022Article
- Photography by Cameras Integrated in Smartphones as a Tool for Analytical Chemistry Represented by an Butyrylcholinesterase Activity Assay.Sensors (Basel, Switzerland) · 2015Article
- Dioxin and dioxin-like compounds suppress acetylcholinesterase activity via transcriptional downregulations in vitro.Journal of molecular neuroscience : MN · 2014Article
- Inhibitors of acetylcholinesterase and butyrylcholinesterase meet immunity.International journal of molecular sciences · 2014Review
- Biodegradation of malathion by Brevibacillus sp. strain KB2 and Bacillus cereus strain PU.World journal of microbiology & biotechnology · 2012Article
- Effects of the Yangtze River source of drinking water on metabolites of Mus musculus.Ecotoxicology (London, England) · 2009Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbofuran and malathion, well known pesticides, and paraquat, a world widely used herbicide, were tested on acetylcholinesterase (AChE) from Bungarus sindanus venom and butyrylcholinesterase (BChE) from human serum. The calculated IC(50 )values for inhibition of venom enzyme by malathion, carbofuran and paraquat were 2.5, 0.14, and 0.16 microM, respectively. The values for inhibition of serum butyrylcholinesterase (BChE) were 3.5, 0.09 and 0.18 microM, respectively. Analysis of kinetic data indicated that the inhibition caused by malathion, carbofuran and paraquat was mixed for venom AChE. For BChE from human serum, the inhibition caused by malathion and paraquat was mixed and for carbofuran it was uncompetitive. The present results suggest a commercial paraquat preparation (a popular herbicide) inhibits cholinesterases with similar or higher potency than classical pesticide inhibitors. Furthermore, this inhibition was observed both in human serum and snake venom, a newly studied source of AChE.
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