Abstract
Glutamate dehydrogenase has been purified to near-homogeneity from mature larvae of Drosophila melanogaster. The enzyme has a molecular weight of 347,000 measured by sucrose gradient sedimentation and 343,000 measured by variable-porosity acrylamide gel electrophoresis. Electrophoresis under denaturing conditions showed that the enzyme consists of six subunits of molecular weight 57,000. The structural gene for GDH has been mapped at 81.7±0.8 on the third chromosome by means of an electrophoretic variant.
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This work was supported by CNR Contract 76-01961-04.
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Caggese, C., De Pinto, V. & Ferrandino, A. Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster . Biochem Genet 20, 449–460 (1982). https://doi.org/10.1007/BF00484696
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DOI: https://doi.org/10.1007/BF00484696