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- W4240469413 abstract "This chapter describes a method for enzymatic determination of α-oxoglutarate. The enzymatic determination of α-oxoglutarate with reduced diphosphopyridine nucleotide (DPNH) and glutamic dehydrogenase was developed by Wallenfels and Christian, after the enzyme had been isolated in a pure state and crystallized. The method was immediately used for metabolic studies because in contrast to the methods then available, it has the advantage of being simple and specific. The method is based on the principle that glutamic dehydrogenase (G1DH) catalyzes the reaction as described in the chapter. With an excess of NH4+ ions and DPNH, α-oxoglutarate is quantitatively converted to glutamate. For each mole of α-oxoglutarate, 1 mole of DPNH is oxidized. The decrease in the optical density at 340 or 366 mμ because of the oxidation of DPNH is a measure of the reaction. The G1DH preparation should have a specific activity of at least 3 units/mg. The maximum allowable contamination with other enzymes is: 0.5% lactic dehydrogenase; 0.15% glycerol 1-phosphate dehydrogenase; 0.15% malic dehydrogenase (relative to the specific activity of the G1DH)." @default.
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- W4240469413 date "1965-01-01" @default.
- W4240469413 modified "2023-09-28" @default.
- W4240469413 title "α-Oxoglutarate" @default.
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- W4240469413 doi "https://doi.org/10.1016/b978-0-12-395630-9.50069-4" @default.
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