Results 261 to 270 of about 158,395 (286)
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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.
K M, Blumenthal, E L, Smith
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Bovine thyroid cytosol glutamate dehydrogenase
Life Sciences, 1973Abstract The distribution of glutamate dehydrogenase in bovine thyroid tissue differs from the distribution observed in other mammalian tissues. While the mitochondria of thyroid tissue contain glutamate dehydrogenase which is ‘activated’ by treatment of the mitochondria with a non-ionic detergent, the majority of the glutamate dehydrogenase activity
J D, Larson, A R, Schulz
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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.
P A, Bond, J H, Sang
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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.
Y, Mohran +4 more
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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 ...
R A, Prough, A H, Colen, H F, Fisher
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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.
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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.
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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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1971
Publisher Summary Glutamate dehydrogenases, as a class, catalyze the reversible oxidative deamination of L-glutamate to α -ketoglutarate and ammonia. The description of the characteristics of this reaction from a variety of sources show that, although all classed as glutamate dehydrogenase, the enzymes are different in terms of kinetic ...
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Publisher Summary Glutamate dehydrogenases, as a class, catalyze the reversible oxidative deamination of L-glutamate to α -ketoglutarate and ammonia. The description of the characteristics of this reaction from a variety of sources show that, although all classed as glutamate dehydrogenase, the enzymes are different in terms of kinetic ...
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