Effects of water pollutants and other chemicals on fish acetylcholinesterase (in vitro)

Brain acetylcholinesterase as a marine pesticide biomarker using Brazilian fishes

“…Variations of physicochemical parameters were very small and even in station B, where the greatest variations were observed, there was no correlation between the physicochemical parameters and AChE activity (Table 2). Similarly, Olson & Christensen (1980) studied the effect of many chemicals in muscle AChE activity in fathead minnow (Pimephales promelas) and found that nitrate above 0.01 M caused a slight inhibition of the enzyme while phosphate and ammonium had no effect, even in concentrations above 0,01 M. In the present work, the concentrations of nitrate, phosphate and ammonium did not exceed 0.01 M in any water sample analyzed.…”

Methylmercury accumulation, histopathology effects, and cholinesterase activity alterations in medaka (Oryzias latipes) following sublethal exposure to methylmercury chloride

“…The irregular patterns were also documented in previous studies. Olson and Christensen (1980) reported that strong and intermediate AChE inhibitions were found in fathead minnow (Pimephales promelas) treated (in vitro) with heavy metal cations and organometals, respectively. Schmidt and Ibrahim (1994) found that the ChE activity was increased to about 14% in adult grasshopper (Aiolopus thalassinus) treated (in vivo) with lead chloride.…”

“…Both AChE and BuChE contribute to ChE activity in aquatic organisms (Sturm et al, 1999(Sturm et al, , 2000. Effects of mercury and its derivatives on ChE activity alteration have been widely reported in many previous works (Olson and Christensen, 1980;Suresh et al, 1992;Schmidt and Ibrahim, 1994;Devi and Fingerman, 1995). By binding of Hg to the sulfhydryl group, mercuric compounds can induce a conformational change in ChE.…”

Effect of ions on the activity of brain acetylcholinesterase from tropical fish

“…Some studies pointed to the influence of ions on the AChE activity by binding to peripheral sites promoting conformational modifications or changing the hydration state of the active center which alters the rate of substrate hydrolysis by the enzyme [12,19,20]. Hughes and Bennett [12] .…”