“…Regardless the types, ChEs are strongly inhibited by anticholinesterases such as organophosphates (OPs) and cabamates (CBs). This allows them to serve as effective biomarkers in the field (SanchezHernandez et al, 1998;Stien et al, 1998;Kirby et al, 2000;den Besten et al, 2001;Forget et al, 2003;Quintaneiro et al, 2006;Jung et al, 2008;Elhalwagy et al, 2010;Sáenz et al, 2010;van Oosterom et al, 2010;Printes et al, 2011).…”
Due to their significant value in both economy and ecology, Daphnia had long been employed to investigate in vivo response of cholinesterase (ChE) in anticholinesterase exposures, whereas the type constitution and property of the enzyme remained unclear. A type of ChE was purified from Daphnia magna using a three-step procedure, i.e., Triton X-100 extraction, ammonium sulfate precipitation, and diethylaminoethyl (DEAE)-Sepharose™-Fast-Flow chromatography. According to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), molecular mass of the purified ChE was estimated to be 84 kDa. Based on substrate studies, the purified enzyme preferred butyrylthiocholine iodide (BTCh) [with maximum velocity (V max )/Michaelis constant (K m )=8.428 L/(min·mg protein)] to acetylthiocholine iodide (ATCh) [with V max /K m =5.346 L/(min·mg protein)] as its substrate. Activity of the purified enzyme was suppressed by high concentrations of either ATCh or BTCh. Inhibitor studies showed that the purified enzyme was more sensitive towards inhibition by tetraisopropylpyrophosphoramide (iso-OMPA) than by 1,5-bis(4-allyldimethylammoniumphenyl) pentan-3-one dibromide (BW284C51). Result of the study suggested that the purified ChE was more like a type of pseudocholinesterase, and it also suggested that Daphnia magna contained multiple types of ChE in their bodies.
“…Regardless the types, ChEs are strongly inhibited by anticholinesterases such as organophosphates (OPs) and cabamates (CBs). This allows them to serve as effective biomarkers in the field (SanchezHernandez et al, 1998;Stien et al, 1998;Kirby et al, 2000;den Besten et al, 2001;Forget et al, 2003;Quintaneiro et al, 2006;Jung et al, 2008;Elhalwagy et al, 2010;Sáenz et al, 2010;van Oosterom et al, 2010;Printes et al, 2011).…”
Due to their significant value in both economy and ecology, Daphnia had long been employed to investigate in vivo response of cholinesterase (ChE) in anticholinesterase exposures, whereas the type constitution and property of the enzyme remained unclear. A type of ChE was purified from Daphnia magna using a three-step procedure, i.e., Triton X-100 extraction, ammonium sulfate precipitation, and diethylaminoethyl (DEAE)-Sepharose™-Fast-Flow chromatography. According to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), molecular mass of the purified ChE was estimated to be 84 kDa. Based on substrate studies, the purified enzyme preferred butyrylthiocholine iodide (BTCh) [with maximum velocity (V max )/Michaelis constant (K m )=8.428 L/(min·mg protein)] to acetylthiocholine iodide (ATCh) [with V max /K m =5.346 L/(min·mg protein)] as its substrate. Activity of the purified enzyme was suppressed by high concentrations of either ATCh or BTCh. Inhibitor studies showed that the purified enzyme was more sensitive towards inhibition by tetraisopropylpyrophosphoramide (iso-OMPA) than by 1,5-bis(4-allyldimethylammoniumphenyl) pentan-3-one dibromide (BW284C51). Result of the study suggested that the purified ChE was more like a type of pseudocholinesterase, and it also suggested that Daphnia magna contained multiple types of ChE in their bodies.
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