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- W2062360119 abstract "l-Alanine aminotransferase (E.C. 2.6.1.2.) has been isolated from imagines of Drosophila nigromelanica. The specific activity of the enzyme is 486 U/mg protein which corresponds to a 1200-fold purification. Only a single native form of the enzyme was found. The molecular weight has been determined to be 113,000 by gel filtration, and 56,000 by SDS gel electrophoresis. Thus it is concluded that the native enzyme consists of two subunits of equal molecular weight. The kinetics of transamination was studied in both directions. The results showed that Drosophila l-alanine aminotransferase has also the ping-pong mechanism of catalysis that has been suggested for the same enzyme from mammals. The absolute Michaelis constants are: l-alanine, 5.2 mM; α-ketoglutarate, 0.43 mM; l-glutamate, 14 mM; pyruvate, 0.25 mM. The overall results indicated that l-alanine aminotransferase in Drosophila possesses very similar properties as the mammalian enzyme. During larval development the level of enzyme activity increases rapidly until pupation, declines to a minimum at the middle of pupal life, and rises again shortly before and after adult emergence. The enzyme activities in different adult organs and tissues of mated and unmated flies were also determined. The results are discussed in view of the metabolic roles of l-alanine aminotransferase in protein synthesis and gluconeogenesis." @default.
- W2062360119 created "2016-06-24" @default.
- W2062360119 creator A5029759771 @default.
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- W2062360119 date "1981-01-01" @default.
- W2062360119 modified "2023-10-16" @default.
- W2062360119 title "l-Alanine aminotransferase in Drosophila nigromelanica: isolation, characterization and activity during ontogenesis" @default.
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- W2062360119 doi "https://doi.org/10.1016/0020-1790(81)90056-1" @default.
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