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Pyrethroid-hydrolyzing esterases in southern armyworm larvae: Tissue distribution,kinetic properties,and selective inhibition
Authors:Yehia AI Abdel-Aal  David M Soderlund
Institution:Department of Entomology, New York State Agricultural Experiment Station, Cornell University, Geneva, New York 14456 USA
Abstract:Esterase activity hydrolyzing both 1RS,trans]- and 1RS,cis]-permethrin was detected in crude homogenates of the following southern armyworm (Spodoptera eridania Cramer) larval tissues: cuticle, gut, fat body, head capsule, Malpighian tubules, and silk gland. Neither substrate was detectably hydrolyzed by hemolymph. The highest esterase activities per insect equivalent of tissue were found in cuticle, gut, and fat body for the trans isomer and in cuticle and gut for the cis isomer. Each preparation hydrolyzed the trans isomer more rapidly, but the degree of specificity varied greatly between tissues. Differences in apparent Km and Vmax values between the three most active tissues were threefold or less for trans isomer hydrolysis, but differences between tissues of up to 100-fold were found for Km and Vmax values for cis isomer hydrolysis. Hydrolysis of the trans isomer in cuticle, gut, and fat body homogenates was only partially inhibited by α-naphthyl N-propylcarbamate (NPC). Concentrations of NPC giving maximal inhibition of trans isomer hydrolysis had little effect on the hydrolysis of the cis isomer. These results demonstrate that pyrethroid-hydrolyzing activity is broadly distributed in insect tissues and results from the combined activity of several esterases with different properties. It is likely that the trans and cis isomers of permethrin are hydrolyzed by separate enzymes in this insect.
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