The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea. From the mollusk, molecular forms of acetylcholinesterase (AChE), consisting of two prevailing spontaneously soluble (SS) forms present in the blood, were obtained. These forms are a globular tetramer (SSG4), a dimer (SSG2) of catalytic subunits, and a minor amphiphilic globular dimer (low-salt Triton [LST] G2) phosphatidylinositol tailed. All SS and LST forms, partially purified by affinity chromatography, are AChEs with a marked substrate specificity for acetylthiocholine and poor hydrolysis with butyrylthiocholine. They are poorly inhibited by carbamate eserine and show a different pattern of inhibition by organophosphate diisopropylfluorophosphate (DFP), with totally resistant SS forms from clams collected from the two stations nearest the Po River. Acetylcholinesterase SS and LST forms are expressed at highest, lowest, and middle levels in clams collected from the northern station, closer to the Po delta, and from the two more southern ones, respectively. The possibility that the expression pattern of AChE forms is due to effects of single or mixed classes of chemical pollutants is discussed.
Different expressions of organophosphate-resistant acetylcholinesterases in the bivalve mollusk Scapharca inaequivalvis living in three different habitats.
TALESA, Vincenzo Nicola;ROMANI, Rita;ANTOGNELLI, Cinzia;GIOVANNINI, Elvio;ROSI, Gabriella
2002
Abstract
The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea. From the mollusk, molecular forms of acetylcholinesterase (AChE), consisting of two prevailing spontaneously soluble (SS) forms present in the blood, were obtained. These forms are a globular tetramer (SSG4), a dimer (SSG2) of catalytic subunits, and a minor amphiphilic globular dimer (low-salt Triton [LST] G2) phosphatidylinositol tailed. All SS and LST forms, partially purified by affinity chromatography, are AChEs with a marked substrate specificity for acetylthiocholine and poor hydrolysis with butyrylthiocholine. They are poorly inhibited by carbamate eserine and show a different pattern of inhibition by organophosphate diisopropylfluorophosphate (DFP), with totally resistant SS forms from clams collected from the two stations nearest the Po River. Acetylcholinesterase SS and LST forms are expressed at highest, lowest, and middle levels in clams collected from the northern station, closer to the Po delta, and from the two more southern ones, respectively. The possibility that the expression pattern of AChE forms is due to effects of single or mixed classes of chemical pollutants is discussed.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.