Properties of the Aldrin Epoxidase System in the Gut and Fat Body of a Caddisfly Larval1

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Abstract
Aldrin epoxidation was used as an index of mixed function oxidase activity in gut and fat body homogenates of a caddisfly Lanva, Limnephilus sp., and the transformation of aid rill to dieldrin also was demonstrated in, vivo, whole larval homogenates were unsuitable enzyme sources, because the gut content contained a soluble, heat-labile inhibitor of epoxidation. Gut and fat body preparations required reduced nicotinamide adenine dinudeotide phosphate for maximum catalytic activity, and epoxidation was reduced by carbon monoxide, sesamex, and SKF 525-A (2-(diethylamine) ethyl 2.2-diphenylvalerate hydrochloride). Bovine serum albumin increased the rate of epoxiclation in gut preparations to a greater extent than it did with fat body preparations. Each homogenate was more active in tris-HCl than in phosphate buffer, and the epoxidase systems were inactivated irreversibly when incubated above 30°C.

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