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Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by(More)
When Drosophila melanogaster larvae were fed a defined fat-free, low sucrose medium, alcohol dehydrogenase (ADH) was increased to a higher activity with a moderate, nontoxic level of ethanol (2.5% vol/vol) within 5 h. Ethanol-stimulated increases in ADH activity and cross-reacting material in late third-instar larvae were paralleled by increases in the(More)
The tissue activities of the oxidative pentose shunt enzymes, glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) and 6-phosphogluconate dehydrogenase (E.C. 1.1.1.44), in the larvae of Drosophila melanogaster are not dependent on the amount of flux through the oxidative pentose shunt pathway. An oxidative pentose shunt deficiency effects about a 40% reduction(More)
NADP-malic enzyme (NADP-ME) (E.C. 1.1.1.40) is situated in the cytosol of Drosophila melanogaster. Both the tissue activity and CRM level of NADP-ME parallel changes in the dosage of a gene, Men+, located in region 87C2-3 to 87D1-2 of the third chromosome. The tissue activity of NADP-ME is very high in early third instar larvae, providing about 33% of the(More)
The activity of alcohol dehydrogenase (ADH:EC 1.1.1.1), the initial enzyme in the major pathway for ethanol degradation, is induced in Drosophila melanogaster larvae by low concentrations of dietary ethanol. Two lines of evidence indicate that the metabolic products of the ADH pathway for ethanol degradation are not directly involved in the induction of(More)
Dietary sucrose and ethanol are potent modulators of sn-glycerol-3-phosphate dehydrogenase (GPDH) in the third instar larvae of Drosophila melanogaster. When added to modified Sang's medium C, 428 mM ethanol and 146 mM sucrose each increased the GPDH tissue activity more than 90% and GPDH cross-reacting material (CRM) more than 50% over the levels found in(More)
In Drosophila melanogaster aldehyde oxidase occurs in at least two forms that can be separated electrophoretically. The mutant allele lao (low aldehyde oxidase activity) causes a deficiency of the major form of this enzyme. Immunoelectrophoretic analyses suggest that lao homozygotes produce aldehyde oxidase cross-reacting-material in nearly wild-type(More)
Four-day post-hatch larvae (mid-third instar) of Drosophila melanogaster were fed an intermediate diet with or without supplement of an individual fatty acid for 2 d and then transferred to a diet with a growth-limiting level of 0.94 mol/L ethanol (5.5%, v/v) or an ethanol-free diet. The ethanol stress decreased survival and larval development rate but(More)
Wild-type third instar larvae of Drosophilia melanogaster fed a casein-sucrose synthetic diet supplemented with phosphatidylcholine (4 mg/ml) possessed 33% more tissue lipid and a modified fatty acid profile compared to larvae fed a fat free-sucrose diet. The rates of lipid synthesis and pentose shunt activity were 2.1 and 2.2 times greater respectively in(More)