RESUMO
Mitochondrial and cytoplasmic isozymes of arginine kinase have been identified in Drosophila melanogaster. On the basis of their immunological similarity, parallel dosage responses, and cosegregation of electrophoretic mobility differences, it is concluded that both isozymes are the product of a single gene. The consequences of this in relation to the regulation and evolution of this unusual gene-enzyme system are discussed. It is inferred that the origin of the phosphagen shuttle must predate the divergence of invertebrates and vertebrates.
Assuntos
Arginina Quinase/genética , Drosophila melanogaster/genética , Genes , Mitocôndrias/enzimologia , Fosfotransferases/genética , Animais , Arginina Quinase/metabolismo , Cruzamentos Genéticos , Drosophila melanogaster/enzimologia , Feminino , Homozigoto , Masculino , FenótipoRESUMO
Phosphofructokinase (PFK;EC 2.7.1.11) activity in Drosophila melanogaster is controlled by a single dosage-sensitive region of the genome between 45F and 47E of chromosome IIR. Only a single form of PFK was detected electrophoretically in both adults and larvae. Nearly 90% of the PFK activity in adults is localized to the thorax. Purification of the enzyme was hampered by the extreme lability of Drosophila PFK; however, a 36-fold partial purification was achieved.
