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Comparative analysis of malate dehydrogenases of Drosophila melanogaster

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Abstract

The malate dehydrogenases of D. melanogaster have been resolved into a cytoplasmic form (cMDH) and a mitochondrial matrix form (mMDH). Flies homozygous for allozyme variants exhibit isozymes of cMDH detected by starch gel electrophoresis and acrylamide gel isoelectric focusing. The basis of these isozymes was investigated, and the results suggest either conformational or epigenetic modification of isozymes. The probable structural gene for cMDH (Mdh-1) has been mapped genetically by allozyme variants to II-35 ± 3 and cytologically by monitoring gene dosage in segmental aneuploids to between 28D and 29F on II-L of the Drosophila salivary gland chromosome map. The structural gene for mMDH is neither identical to nor in the near chromosomal proximity of Mdh-1. Nevertheless, the two enzymes exhibit markedly similar properties with respect to (1) catalytic activity, (2) pH optima, (3) pH optimum shift in response to different ionic environments, and (4) molecular weight as determined by sucrose density gradient sedimentation.

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Author notes

  1. Stephen J. O'Brien

    Present address: Cell Biology Section, Viral Biology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland

Authors and Affiliations

  1. Gerontology Research Center, National Institute of Child Health and Human Development, National Institutes of Health, Baltimore City Hospitals, Baltimore, Maryland

    Stephen J. O'Brien

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  1. Stephen J. O'Brien
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Additional information

This project was supported by NIH postdoctoral research fellowship No. 6-FO2-GM-49, 633-01 from the National Institute of General Medical Sciences.

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O'Brien, S.J. Comparative analysis of malate dehydrogenases of Drosophila melanogaster . Biochem Genet 10, 191–205 (1973). https://doi.org/10.1007/BF00485765

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  • DOI: https://doi.org/10.1007/BF00485765

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