Results 231 to 240 of about 87,161 (272)
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Glutamine synthetase deadenylylating enzyme
Biochemical and Biophysical Research Communications, 1968The glutamine synthetase of Escherichiacoli exists in various forms differing from each other by their content of covalently bound adenylyl groups (Shapiro etal., 1967;Wulff etal., 1967). The biosynthetic activity of unadenylylated glutamine synthetase is very much greater with Mg2+ as the activating cation than with Mn2+, and its γ-glutamyl ...
B M, Shapiro, E R, Stadtman
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Glutamine synthetase deficiency
2020Prenatal onset malformations of the brain, seizures, necrolytic erythema of the skin, enteropathy with diarrhea, early neonatal death, and multiorgan failure or chronic encephalopathy and developmental delay, hyperammonemia, low concentration of glutamine in plasma and cerebrospinal fluid, and deficient activity of glutamine synthetase.
William L. Nyhan +3 more
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Equine placenta expresses glutamine synthetase
Veterinary Research Communications, 2008In most mammalian species the developing fetus utilizes large amounts of glutamine derived both from the maternal circulation and synthesized de novo in the placenta. The present study was designed to determine the role of the placenta in glutamine synthesis in the horse.
Hélio C, Manso Filho +4 more
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Regulation of Glutamine Synthetase Activity
EcoSal Plus, 2004Detailed studies of the glutamine synthetase (GS) in Escherichia coli and other bacteria have shown that the activity of this enzyme is regulated by at least five different mechanisms: (i) cumulative feedback inhibition by multiple end products of glutamine metabolism, (ii) interconversion between taut and relaxed ...
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[Glutamine synthetase immobilization].
Prikladnaia biokhimiia i mikrobiologiia, 1978Highly purified glutamine synthetase has been isolated from Chlorella and immobilized on BrCN-sepharose. Its residual activity was 25-35%. Immobilized glutamine synthetase showed far greater thermal stability than glutamine synthetase in solution. During immobilization pH optimum of the enzyme was shifted towards the alkaline area, maximum rate of the ...
A S, Rasulov, Z G, Evstigneeva
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Intrahippocampal kainic acid reduces glutamine synthetase
Neuroscience, 1990Kainic acid was injected into the hippocampus of rats and glutamine synthetase was measured to determine whether astrocytes are involved in the early effects of this neurotoxic agent. Glutamine synthetase was reduced by 38%, 24 h after the stereotaxic application of 4 nmol of kainic acid to this region.
R A, Waniewski, D, McFarland
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Localisation of Glutamine Synthetase in Chloroplasts
Nature New Biology, 1973Glutamine is of considerable importance in plants, as a readily metabolised and translocated intermediate and as a product of ammonia detoxification. Glutamine synthetase carries out the ATP-driven addition of ammonia to glutamate to produce the amide. The source of ATP and information on the metabolic role, for glutamine synthetase may be suggested by
D, O'Neal, K W, Joy
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Glutamine Synthetase: Glial Localization in Brain
Science, 1977Light microscopy immunohistochemical techniques were used to examine the distribution of glutamine synthetase in rat brain. Glutamine synthetase was found to be localized in the glial cells. Neuronal cell bodies, endothelial cells, and choroid epithelium contained no enzyme.
A, Martinez-Hernandez +2 more
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Inhibitors of Glutamine Synthetase
2002Due to the chemical inertness of the N2 molecule, the availability of metabolically accessible inorganic nitrogen sources was a key limiting factor for plant life on earth. The large scale conversion of N2 into NH3 and NO 3 - and their use as nitrogen fertilizer has been an agricultural standard for less than a century.
Guenter Donn, Helmut Köcher
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Glutamine synthetase and transferase
1967This enzyme (or enzymes) catalyzes the following reactions: 1. Glutamate + ATP + NH3 → glutamine + ADP + Pi (glutamine synthesis). 2. Glutamine + NH2OH →γ-glutamylhydroxamate + NH3 (glutamyl transfer reaction). 3. Glutamine + H2O → Glutamate + NH3 (arsenolysis of glutamine).
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