Showing papers on "Acetylthiocholine published in 2014"
TL;DR: A fluorescein-based sensor was developed for the AChE activity assay and the inhibitor screening and provided the dual assay methods for the screening of A ChE activity in the presence or absence of inhibitor.
21 citations
TL;DR: This study suggests that AChE activity in caddisflies can indeed be used to discriminate the effects of specific insecticides in monitoring programs and the use of non-target species such as c addisflies in ecotoxicological research in lotic ecosystems is discussed.
15 citations
TL;DR: The interactions observed between the substrates of AChE and PVase suggest that part of PVase activity might be a protein with acetylthiocholine-hydrolyzing activity.
11 citations
TL;DR: The sensitivity of cholinesterase activity in plasma of rabbits following both in vivo and in vitro exposure to sub-lethal concentrations of diazinon is demonstrated and is demonstrated to be similar to pre-administration.
7 citations
TL;DR: A single-chain variable fragment library is used to select a recombinant antibody fragment with butyrylcholinesterase-like catalytic activity by using an innovative method integrating genetic selection and the bait-and-switch strategy, and a hypothetical 3D structure of the WZ1–14.2.1 catalytic site is proposed on the basis of a molecular modeling analysis.
Abstract: Organophosphates are potent poisoning agents that cause severe cholinergic toxicity. Current treatment has been reported to be unsatisfactory and novel antidotes are needed. In this study, we used a single-chain variable fragment (scFv) library to select a recombinant antibody fragment (WZ1–14.2.1) with butyrylcholinesterase-like catalytic activity by using an innovative method integrating genetic selection and the bait-and-switch strategy. Ellman assay demonstrated that WZ1–14.2.1 has Michaelis-Menten kinetics in the hydrolysis of all the three substrates used, acetylthiocholine, propionylthiocholine and butyrylthiocholine. Notably, the catalytic activity was resistant to the following acetylcholinesterase inhibitors: neostigmine, iso-OMPA, chlorpyrifos oxon, dichlorvos, and paraoxon ethyl. Otherwise, the enzymatic activity of WZ1–14.2.1 was inhibited by the selective butyrylcholinesterase inhibitor, ethopropazine, and by the Ser-blocking agent phenylmethanesuphonyl fluoride. A hypothetical 3D structure of the WZ1–14.2.1 catalytic site, compatible with functional results, is proposed on the basis of a molecular modeling analysis.
3 citations