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Glutamate oxidation in astrocytes: Roles of glutamate dehydrogenase and aminotransferases
Journal of Neuroscience Research, 2016The cellular distribution of transporters and enzymes related to glutamate metabolism led to the concept of the glutamate–glutamine cycle. Glutamate is released as a neurotransmitter and taken up primarily by astrocytes ensheathing the synapses. The glutamate carbon skeleton is transferred back to the presynaptic neurons as the nonexcitatory amino acid
McKenna, Mary C +5 more
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Glutamate dehydrogenase of Tetrahymena
Biochimica et Biophysica Acta (BBA) - Enzymology, 1974Abstract Glutamate dehydrogenase [ l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis . The activity with the four pyridine nucleotide substrates was catalyzed by a single enzyme as indicated by the
Kenneth Kemp +2 more
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Studies of Glutamate Dehydrogenase
European Journal of Biochemistry, 1973Specific interaction between α‐NADH and glutamate dehydrogenase is demonstrated by difference spectroscopy, circular dichroism and fluorescence measurements. Quantitative binding studies in the preparative ultracentrifuge yield six identical α‐NADH binding sites per oligomer with a dissociation constant of 20 μM.
Rudolf Koberstein +2 more
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Glutamate dehydrogenase-malate dehydrogenase complex
Archives of Biochemistry and Biophysics, 1979Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
Linda Lou Smith +2 more
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Glutamate dehydrogenase of Sphagnum
Phytochemistry, 1997Abstract Glutamate dehydrogenase (GDH) of S. fallax was purified 2000-fold to apparent homogeneity. As estimated by gel filtration and SDS-PAGE, a native molecular weight of M r 210 000 and a subunit molecular weight of M r 52 000 were determined, indicating that the enzyme is tetrameric with subunits of identical molecular weights.
Jóska Gerendás +3 more
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Kinetic mechanism of glutamate dehydrogenase
Biochemistry, 1980Initial velocity patterns and dead-end inhibition studies with oxalylglycine suggest that the addition of NADPH, keto acid, and ammonia occurs with obligatory order. For monocarboxylic keto acids, the keto acid-ammonia initial velocity pattern is equilibrium ordered because koff is much greater than Vmax.
James E. Rife, W. W. Cleland
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Allosteric Transitions of Glutamate Dehydrogenase
Nature, 1968L-GLUTAMATE dehydrogenase from beef liver, GDH (EC 1.4.1.3), has a molecular weight of 310,000 (referred to as the oligomer) consisting of six identical subunits1 and six active sites2.
A. D. B. Malcolm, George K. Radda
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Folates as inhibitors of glutamate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976Folates and tetrahydrofolates inhibit beef liver glutamate dehydrogenase (EC 1.4.1.2). Double reciprocal plats indicate a competitive inhibition for alpha-ketoglutarate-glutamate by folic acid and methotrexate and a complex or mixed type for NAD-NADH site. Pteroic acid is not inhibitory at the concentrations studied.
C.L. Krumdieck +2 more
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