Abstract
Soybean root homogenates were found to oxidize aldicarb to aldicarb sulfoxide. Fractionation of soybean root homogenate indicates that the enzyme(s) which oxidize aldicarb to the sulfoxide are largely (63%) in the 25,000 g supernatant. In vitro studies of the 25,000 g supernatant showed a linear reaction rate at 24 and 34°C for periods of up to 2 and 1 hr, respectively, at the pH optimum of 5.5. Bean and soybean root 25,000 g supernatants were the most active on a per milligram of protein basis followed by corn, sorghum, barley, and tomato (8–27 nmol/mg of protein/hr). A 140-fold purification of soybean root aldicarb sulfoxidase was achieved. In vitro studies indicated that methomyl, methiocarb, phorate, Counter, fensulfothion, fenthion, Nemacur, EPTC, vernolate, carboxin, dl-methionine, l-cysteine, l-methionyl- l-serine, thiodiglycolic acid, lipoic acid, thiourea, and thioacetic acid when present at a 10:1 ratio with aldicarb significantly inhibited soybean root aldicarb sulfoxidation.
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