The occurrence and comparative activity of glycoside conjugating enzymes were investigated in insect and vertebrate species. Although some quantitative differences were noted, all species readily conjugated the substrate, 1-naphthol. Glucosyltransferase activity was essentially the same in whole body homogenates and in selected tissues of the adult housefly, Musca domestica L., and the American cockroach, Periplaneta americana (L.), and larvae of the alfalfa weevil, Hyper postica (Gyllenhal), tobacco hornworm, Manduca sexta (L.), and Indian meal moth, Plodia interpunctella (Hübner). In the rat, the comparable enzyme, glucuronyltransferase, was more active in the liver, kidney, and lungs than in the intestine, stomach, heart, fat, and brain. Glycoside conjugating enzymes were stable when stored in the intact tissue or in various subcellular fractions at −20° and O°C for 90 days. In vitro glucosylation of 1-naphthol by house flies was not influenced by developmental state, age, sex or insecticide resistance.
Document Type: Research Article
Publication date: June 1, 1974
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