Abstract
No less than twelve separate esterolytic enzymes were disclosed by the electrophoretic analysis of the supernatant fraction from whole cockroach homogenates. These isolated enzymes exhibited definite substrate preferences, and the effect of various inhibitors indicated the presence of five different organophosphorus resistant esterases and six separate ali-esterases in addition to cholinesterase. The dissected tissues of the cockroach were assayed colorimetrically for esterase activity with alpha-naphthyl acetate as substrate. The nerve cord and the brain were the sites of greatest activity. The other tissues in the order of decreasing enzyme activity were: midgut, Malpighian tubules, fat body, foregut, hindgut, haemolymph, reproductive system, and muscle. The largest number and the major concentration of the organophosphorus resistant esterases were found in the alimentary tract and the haemolymph, while the most abundant number and amount of the aliesterases were observed in the nerve cord, brain, fat body, and integument. Cholinesterase appeared to be restricted to the nervous system. The results of injection studies revealed that TOCP is not a selective inhibitor for aliesterases in vivo.
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