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Alternative substrates for glutamate dehydrogenases
Biochemical and Biophysical Research Communications, 1975Summary The amide group of glutamine functions as a nitrogen donor in the reactions catalyzed by both the NADP-specific glutamate dehydrogenase of Neurospora crassa and the bovine liver enzyme, but not by the NAD-specific Neurospora enzyme. Asparagine serves as nitrogen source only for the NADP-specific Neurospora dehydrogenase.
Emil L. Smith, Kenneth M. Blumethal
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Chymotryptic activation of glutamate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983Treatment of bovine liver glutamate dehydrogenase (L-glutamate:NAD(P)+ oxidoreductase (deaminating), EC 1.4.1.3) with chymotrypsin generates a proteolytic derivative that is activated 3-4-fold over the native enzyme. Stable preparations of activated enzyme show altered kinetic parameters (5-fold increase in Km for glutamate, 3-fold increase in Vmax ...
Robert J. Beynon, Graham A. Place
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The Radiation Inactivation of Glutamate Dehydrogenase
Radiation Research, 1983Pulse radiolysis and 60Co gamma radiolysis were used to study the effects of ionizing radiations on the activity of glutamate dehydrogenase. Hydroxyl radicals are considerably more effective than hydrated electrons in causing loss of enzymatic activity. Evidence is also presented that the free radical anions (SCN)-.2, (Br)-.2, and (I)-.2 react with the
Radwan R. Abu El Failat +2 more
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1975
Publisher Summary This chapter discusses the types of investigations with major emphasis on recent studies that include elucidation of complete or partial amino acid sequences of the enzymes from several sources. L-Glutamate dehydrogenases catalyze the interconversion of α-ketoglutarate and L-glutamic acid.
Emil L. Smith +3 more
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Publisher Summary This chapter discusses the types of investigations with major emphasis on recent studies that include elucidation of complete or partial amino acid sequences of the enzymes from several sources. L-Glutamate dehydrogenases catalyze the interconversion of α-ketoglutarate and L-glutamic acid.
Emil L. Smith +3 more
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Bovine Liver Glutamate Dehydrogenase
1976Publisher Summary This chapter discusses the current ideas on the catalytic reaction of glutamate dehydrogenase, including its mechanism and regulation, substrate inhibition or activation, the binding of coenzymes to the enzyme, the effect of purine nucleotides, and the mechanism of ligand-induced structural changes.
Robert Josephs +2 more
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A kinetic model for glutamate dehydrogenase
Journal of Theoretical Biology, 1977Abstract A model for the glutamate dehydrogenase reaction has been obtained that contains the reported intermediates suggested by binding and equilibrium isotope exchange methods. Calculated steady state-initial velocity rates using this model are quantitatively consistent with a wide range of nonlinear experimental data in both directions.
L.A. Parks +3 more
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Glutamate dehydrogenase of Drosophila larvae
Journal of Insect Physiology, 1968Abstract Larvae of Drosophila contain a glutamate dehydrogenase which is localized mainly in the mitochondria. The enzyme operates with either NAD or NADP as coenzyme, and is unusual in that NAD is more readilyutilized in one reaction whereas NADPH is more efficient in the other.
James H. Sang, Peter A. Bond
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Serum isocitric dehydrogenase and glutamic dehydrogenase in schistosomiasis
Transactions of the Royal Society of Tropical Medicine and Hygiene, 1969Abstract 19 patients with schistosomiasis were studied for serum ICDH and GLDH activities; they were divided into two groups according to the presence or absence of hepatic involvement. Serum ICDH levels were normal, except in one patient with advanced hepatic decompensation.
M.S. Shoeb +4 more
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Activation of glutamate dehydrogenase by l-leucine
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989The activation of glutamate dehydrogenase (L-glutamate: NAD(P)+ oxidoreductase (deaminating), EC 1.4.1.3) by L-leucine has been studied. Apparently homogeneous preparations from ox liver and brain were found to respond similarly. Commercially obtained preparations of the enzyme, which had suffered limited proteolysis during the purification procedure ...
Couée, Ivan, Tipton, K.F.
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Myocardial Glutamate Dehydrogenase Activity
1986Glutamic dehydrogenase (GDH) has not been thought to play an important role in cardiac metabolism in the past. Aspartate aminotransferase was shown to mediate glutamate utilization by mitochondria and there was thought to be little GDH activity in heart mitochondria.1 However, the studies of Godinot et al showed that this enzyme could be purified from ...
Huey G. McDaniel, Ronald L. Jenkins
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