Cholinesterases from the marine mussels Mytilus galloprovincialis Lmk. and M. edulis L. from the freshwater bivalve Corbicula fluminea Müller

Comp Biochem Physiol C Pharmacol Toxicol Endocrinol. 1999 Mar;122(3):353-61. doi: 10.1016/s0742-8413(98)10130-5.


In order to improve the molecular basis for the use of bivalve cholinesterases as a reliable biomarker for aquatic pollution, the polymorphism and characterization of these enzymes in Mytilus edulis, Mytilus galloprovincialis and Corbicula fluminea were investigated. All results are consistent with the presence of only one pharmacological form of cholinesterase in each species. The molecular masses were 180 kDa for the two marine mussels and 240 kDa for C. fluminea. The cholinesterases are anchored to the membrane by a glycosyl inositol phosphate like the Ga form (type I) described in vertebrates. Surprisingly, these cholinesterases were poorly inhibited by organophosphorous compounds compared to enzymes from other sources. This suggests that these bivalves could be used as a biomarker for acute rather than chronic contaminations by anticholinesterase insecticides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biomarkers
  • Cholinesterases / isolation & purification
  • Cholinesterases / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Environmental Monitoring
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism*
  • Kinetics
  • Mollusca / enzymology*
  • Substrate Specificity


  • Biomarkers
  • Isoenzymes
  • Cholinesterases