Registered users receive a variety of benefits including the ability to customize email alerts, create favorite journals list, and save searches.
Please note that a BioOne web account does not automatically grant access to full-text content. An institutional or society member subscription is required to view non-Open Access content.
Contact firstname.lastname@example.org with any questions.
The inhibition kinetics of dichlorvos on carboxylesterase and acetylcholinesterase (AChE) activity extracted from Liposcelis bostrychophila and L. entomophila (Psocoptera: Liposcelididae) were compared. The results showed that L. entomophila had significantly greater specific activity of carboxylesterase than L. bostrychophila (0.045 versus 0.012 µmoles /mg /min). Moreover, the carboxylexterase of L. entomophila showed higher affinity (i.e. lower Km value) to the substrate 1-naphthyl acetate than L. bostrychophila (0.29 versus 0.67 mM). The specific activity and affinity of AChE of the two species were not significantly different. The carboxylesterase of L. bostrychophila was more sensitive to the insecticide dichlorvos than that of L. entomophila. The I50s values of dichlorvos to carboxylesterase for L. bostrychophila and L. entomophila were 1.43 and 3.28 µM, respectively, and to AChE were 324 and 612 nM, respectively. Inhibition kinetics revealed that AChE from L. bostrychophila was 5.8-fold more sensitive to inhibition than AChE from L. entomophila.