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Updated: Aug 4, 2026

Measurement of Carbon Dioxide Production from Radiolabeled Substrates in Drosophila melanogaster
Published on: June 27, 2016
Genetic and biochemical studies on glutamate-pyruvate transaminase from Drosophila melanogaster
Abstract:
We have used electrophoretic variants of glutamate-pyruvate transaminase (GPT, E.C., 2.6.1.2) in Drosophila melanogaster to genetically map the structural gene to position 42.6 on the X chromosome. By pseudodominance tests over several deficiencies we have localized it cytogenetically to the interval 11Fl-2 to 12Al-2. The sedimentation constant (s20,w) of the native enzyme was determined in sucrose density gradients to be 5.9 and the native molecular weight approximately 87,000. The similarity in physical properties to mammalian enzymes suggests that the enzyme may also be dimeric in D. melanogaster.

