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Glutamate Dehydrogenase Reaction as a Source of Glutamic Acid in Synaptosomes
Journal of Neurochemistry, 1991Abstract: The role of the glutamate dehydrogenase reaction as a pathway of glutamate synthesis was studied by incubating synaptosomes with 5 mM15NH4Cl and then utilizing gas chromatography‐mass spectrometry to measure isotopic enrichment in glutamate and aspartate.
Zhi-Ping Lin+4 more
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Spectra of Glutamate Dehydrogenase with Diethylstilbestrol
Archives Internationales de Physiologie et de Biochimie, 1978Glutamate dehydrogenase displays hyperchromicity at 256 nm and at 276 nm upon binding of diethylstilbestrol. Increase in absorbancy is linear at both regions up to 250 micrometer DES, and becomes parabolic at higher concentration of DES. ADP in the presence of DES causes decrease in absorbancy at 256 nm; absorbancy at 276 nm increased by DES is not ...
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Regulation of glutamate dehydrogenase by histidine
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Histidine and its analogs were demonstrated to activate crystalline beef liver glutamate dehydrogenase ( l -glutamate: NAD+ oxidoreductase (deaminating), EC 1.4.1.2). Activation effects were similar to those of other amino acids such as leucine or norvaline, which have been shown previously by others to exert their activating effect with ...
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Spectrophotometric observation of a glutamate dehydrogenase-l-glutamate complex
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Abstract Ultraviolet differential spectroscopic measurements show the existence of a glutamate dehydrogenase ( l -glutamate:NAD(P) + oxidoreductase (deaminating), EC 1.4.1.3)— l -glutamate complex. The spectral features resemble perturbation difference spectra of enzyme aromatic amino acid chromophores and allow the determination of the l ...
Harvey F. Fisher+5 more
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Conformers of Neurospora glutamate dehydrogenase
Journal of Molecular Biology, 1969Abstract Subunits of Neurospora glutamate dehydrogenase were prepared by treating the enzyme with 6 m -urea, 7 m -guanidinium chloride or 0.2% sodium dodecyl sulphate. Antisera were prepared against the enzyme and the various subunits. These antisera were used in anti-enzyme and precipitation studies with the enzyme and the various subunits.
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Archives of Biochemistry and Biophysics, 1981
Abstract When α-ketoglutarate is the substrate, malate is a considerably more effective inhibitor of glutamate dehydrogenase than glutamate, oxalacetate, aspartate, or glutarate. Malate is a considerably poorer inhibitor when glutamate is the substrate.
Leonard A. Fahien+2 more
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Abstract When α-ketoglutarate is the substrate, malate is a considerably more effective inhibitor of glutamate dehydrogenase than glutamate, oxalacetate, aspartate, or glutarate. Malate is a considerably poorer inhibitor when glutamate is the substrate.
Leonard A. Fahien+2 more
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Glutamate Dehydrogenase as a Neuroprotective Target Against Neurodegeneration
Neurochemical Research, 2018A. Kim, Eun Joo Baik
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