Cholinesterase Activity in the Head of Wild Poecilia reticulata from Bahia, Brazil: Biochemical Characterization, Effects of Sample Storage and Normal Range of Activity

Authors

  • C. Stringuetti Institute of Biology, Universidade Federal da Bahia (UFBA), Campus de Ondina, Salvador, BA, Brazil
  • L. Guilhermino Institute of Biology, Universidade Federal da Bahia (UFBA), Campus de Ondina, Salvador, BA, Brazil
  • Eduardo Mendes da Silva Institute of Biology, Universidade Federal da Bahia (UFBA), Campus de Ondina, Salvador, BA, Brazil

DOI:

https://doi.org/10.5132/jbse.2008.01.009

Keywords:

biomarker, cholinesterase, Poecilia reticulata, sample storage conditions

Abstract

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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Published

12-05-2008

How to Cite

Stringuetti, C., Guilhermino, L., & Silva, E. M. da. (2008). Cholinesterase Activity in the Head of Wild Poecilia reticulata from Bahia, Brazil: Biochemical Characterization, Effects of Sample Storage and Normal Range of Activity. Ecotoxicology and Environmental Contamination, 3(1), 57–63. https://doi.org/10.5132/jbse.2008.01.009

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Original Articles