DIFFERENTIAL RESPONSE OF APIS-MELLIFERA ACETYLCHOLINESTERASE TOWARDS PIRIMICARB

THE kinetic analysis of Apis mellifera acetylcholinesterase inhibition by the carbamate pirimicarb showed that native and detergent-solubilized membrane enzyme exhibited slightly different carbamylation kinetics. The acetylcholinesterase form sensitive to phosphatidylinositol-specific phospholipase C(PI-PLC) was carbamylated more rapidly (k(app) = 36.4 x 10(-3) min-1) than the PI-PLC-resistant counterpart (k(app) = 10.13 x 10(-3) min-1) which had a behavior close to that of the soluble tryptic enzyme (k(app) = 11.89 x 10(-3) min-1). A difference in acetylcholinesterase sensitivity towards pirimicarb was also observed between foraging and emerging bees. These results show that the molecular structure, the mode of preparation and the source of acetylcholinesterase from the bee head should be taken into account in accurate toxicological studies.