Partial purification and enzymatic characterization of acetylcholinesterase from the intertidal marine copepod Tigriopus brevicornis |
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Authors: | J Forget G Bocquen |
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Institution: | a Laboratoire de Physiologie des êtres marins, Institut Océanographique, 195 rue Saint-Jacques, F-75005 Paris, France;b Laboratoire d’Ecotoxicologie, IFREMER, rue de l’Ile d’Yeu, 44311 Nantes Cédex 03, France |
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Abstract: | Marine copepods such as Tigriopus brevicornis are widespread along the Atlantic coast of Europe. These minute crustaceans are highly sensitive to contamination and thus serve as useful bioindicators for the monitoring of pollutant effects. The use of decreased cholinesterase (ChE) activity as a subletal biomarker of exposure to neurotoxic supposes that ChE has been defined in copepods. This study reports the partial purification, separation and characterization of ChE extracted from T. brevicornis. This enzyme is apparently an acetylcholinesterase (AChE) since it hydrolyzed acetylthiocholine iodide at a higher rate than other substrates and was inhibited by eserine but not by iso-OMPA. Electrophoretic studies showed that there is probably a single dimeric form defined by its apparent molecular weight (200 kDa) and sensitivity to inhibitors. The kinetic properties of this ChE were compared with those of other invertebrate ChE. |
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Keywords: | Acetylcholinesterase Biochemical characterization Partial purification Copepod Insecticides Pollution monitoring |
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