Abstract
Glucosylation in insects was investigated using tobacco hornworms ( Manduca sexta) as the primary test insect and 1-naphthol- 14C as the substrate. Of 6 common co-factors tested, only UDPG was utilized by the conjugating enzyme system. Neither the hornworm nor housefly enzymes could form the glucuronic acid derivative of 1-naphthol using UDPGA. Centrifugal fractionation of the hornworm homogenates showed that the glucosyltransferase activity was in the 105,000 g soluble fraction. In the housefly, the enzyme activity was associated with the 15,000 g pellet and to a lesser extent with the 105,000 g pellet. In vitro inhibition of the glucosyltransferase by sulphoxide, piperonyl butoxide, and other insecticide synergists was demonstrated.
Published Version
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