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  • 1
    Electronic Resource
    Electronic Resource
    6-Phosphogluconate dehydrogenase from Drosophila melanogaster. I. Purification and properties of the a isozyme (1980)
    Springer
    Biochemical genetics 18 (1980), S. 87-101 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; 6-phosphogluconate dehydrogenase ; isozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract 6-Phosphogluconate dehyrogenase is evident at all developmental stages of Drosophila melanogaster. The activity level is highest in early third instar larvae and declines to a lower, but relatively constant, level at all later stages of development. The enzyme is localized in the cytosolic portion of the cell. The A-isozymic form of 6-phosphogluconate dehydrogenase was purified to homogeneity and has a molecular weight of 105,000. The enzyme is a dimer consisting of subunits with molecular weights of 55,000 and 53,000. For the oxidative decarboxylation of 6-phosphogluconate the Km for substrate is 81 µm while that for NADP+ is 22.3 µm. The optimum pH for activity is 7.8 while the optimum temperature is 37 C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504362
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  • 2
    Electronic Resource
    Electronic Resource
    Differential characterization of two leucine aminopeptidases in Drosophila melanogaster (1981)
    Springer
    Biochemical genetics 19 (1981), S. 47-60 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; aminopeptidases ; leucine aminopeptidases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two leucine aminopeptidases from Drosophila melanogaster larvae have been partially purified. The LAP A and D enzymes have similar biochemical characteristics including molecular weights of ≅280,000 daltons, Michaelis-Menten constants of ≅0.05 mM, associations with metal cofactors, and specificities toward natural and chromogenic substrates. They differ in their pH optima and spatial distributions. If the closely linked genes that code for these enzymes have resulted from a tandem gene duplication event, it is suggested that there has been subsequent evolutionary divergence. This would provide Drosophila larvae with two related, but functionally distinct enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486136
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a low-activity allele of NADP+-dependent isocitrate dehydrogenase from Drosophila melanogaster (1983)
    Springer
    Biochemical genetics 21 (1983), S. 725-733 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; NADP+-dependent isocitrate dehydrogenase (NADP-IDH) ; cis-acting regulation ; population null alleles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have characterized biochemical effects of Idh GB1 in Drosophila melanogaster. This is a “null”-activity allele for NADP+-dependent isocitrate dehydrogenase (NADP-IDH) isolated from a natural population. The homozygous mutant strain has 5% of the NADP-IDH specific activity found in controls and less than 24% of the immunologically cross-reacting material (CRM). This mutation maps to 27.2 on the third chromosome, to the right of h. The biochemical phenotype of this mutant strain includes a coordinate reduction in malic enzyme (ME) specific activity and CRM and an increase in specific activity for the pentose-phosphate shunt enzymes, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase. The K m values for purified NADP-IDH are not different from those found for the purified control enzyme for NADP+ or isocitrate. It is suggested that this allele may represent a cis-acting control mutation for one of at least two loci involved in the production of NADP-IDH in D. melanogaster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498919
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  • 4
    Electronic Resource
    Electronic Resource
    Comparative properties of three forms of glucose-6-phosphate dehydrogenase in Drosophila melanogaster (1983)
    Springer
    Biochemical genetics 21 (1983), S. 1153-1166 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; glucose-6-phosphate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three alleles of the Zw locus of Drosophila melanogaster—Zw A, ZwB,and Zw lol—apparently code for dimeric, tetrameric, and monomeric forms of glucose-6-phosphate dehydrogenase (G6PD), respectively. The three forms of G6PD are characterized by different apparent K mvalues for glucose-6-phosphate but similar apparent K mvalues for NAPD+. When high concentrations of NAPD+ were added to enzyme preparations, the Zw Aand Zw lolforms of G6PD assumed tetrameric and dimeric properties, respectively. Although Zw loladults exhibit little G6PD activity, they maintain levels of G6PD-antigen comparable to those in Zw Aand Zw Badults. Thus the low level of G6PD activity in Zw lolindividuals cannot be explained as the consequence of lack of synthesis of the G6PD subunit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00488467
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