In this study, the soluble cholinesterases (ChE) from the head of Poecilia reticulata from a wild population of Bahia, Brazil were characterized using different substrates (acetylthiocoline, butyrylthiocoline and proprionylthiocoline) and selective inhibitors (eserine sulphate, iso-OMPA and BW284C51). Possible effects of time (1, 2, 3, and 4 weeks) and different storage temperatures (freezer storage at ca.-20ºC and-50ºC, and liquid nitrogen system at-196ºC) on ChE activity were also investigated, together with the normal range of ChE activity of non-exposed individuals. The results for the enzymatic characterization indicate that the enzyme present in the head of P. reticulata was mainly acetylcholinesterase. The mean and standard deviation of activity found in non-exposed wild males collected in different periods of the year were 149.71 ± 7.72 SD U/mg protein, respectively. ChE activity significantly decreased after the seventh day of sample storage, independently of the temperature.
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