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- W2017335008 abstract "Abstract 1. 1. The ammonia-excreting South African clawed toad Xenopus laevis has a higher activity of glutamate dehydrogenase in the kidney than have other frogs. 2. 2. The kinetics and mechanism of action of glutamate dehydrogenase from the kidney of Xenopus laevis have been investigated. The effects of varying concentrations of NAD and glutamate on the velocity of glutamate oxidation and of varying the concentration of NADH, α-ketoglutarate and ammonium on the rate of glutamate synthesis were studied. Product inhibition studies in the direction of glutamate oxidation were performed. In addition, the rate of isotope exchange between [ 14 C] labelled glutamate and α-ketoglutarate was studied. The results are consistent with an ordered mechanism, with the probable order of addition of substrates in the direction of α-ketoglutarate reduction being NADH, α-ketoglutarate and finally ammonium ion. 3. 3. Compared to the bovine enzyme, Xenopus glutamate dehydrogenase has a high Michaelis constant for ammonium, and a low one for glutamate. This suggests that the function of glutamate dehydrogenase in Xenopus kidney is the formation of excretory ammonia." @default.
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- W2017335008 date "1974-11-01" @default.
- W2017335008 modified "2023-09-27" @default.
- W2017335008 title "A kinetic study of glutamate dehydrogenase from Xenopus laevis" @default.
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- W2017335008 doi "https://doi.org/10.1016/0020-711x(74)90113-x" @default.
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