Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In fetal livers of both man and rat thymidine kinase activity was 12 times higher than in the adult, glutamate dehydrogenase and arginase were present at 20-50% of their adult values, whereas alanine aminotransferase activity was only an insignificant fraction of that in the adult. Although the developmental changes for the four enzymes were quantitatively similar in both species, qualitatively there were some significant differences. In adult human liver, glutamate dehydrogenase activity was distributed almost equally between the cytosol and particles; the concentration of only the soluble enzyme increased after birth. In rat liver, glutamate dehydrogenase remained exclusively a particulate enzyme. The soluble hepatic alanine aminotransferase activity rose in both species after birth (from less than 2 U/g to 41-57 U/g, respectively). Thymidine kinase was wholly soluble in the fetal livers; only in adult human liver was additional activity (at least 50% of the total) found in the particles. Arginase isozymes, identical and apparently the same single isozyme in fetal and adult rat liver, show an ontogenetic change in man. A shift from a single form, common to human fetal liver and fetal kidney, to at least two variants in adult human liver, indicates another complexity of the fully differentiated liver in man.
Pediatr Res 1976 Dec
PMID:Glutamate dehydrogenase, alanine aminotransferase, thymidine kinase, and arginase in fetal and adult human and rat liver. 99 99

With the aid of cytophotometry the author studied the cellular chemistry of neurons (according to the activity of glutamate dehydrogenase) in the III, IV and V layers of the visual cortex in rats during the period of rehabilitation of specific functions following long-term light deprivation. It was demonstrated that a 2-week stay of deprivated animals in conditions of usual light is accompanied by visible normalization of the glutamate dehydrogenase activity in the cortical neurons. However, a complete rehabilitation of the control level was not attained. The study demonstrated differences in the reactions of identical neurons in the IV and V layers to the rehabilitation of specific functions. It is being assumed that the rehabilitation of the visual function may be due to biochemical reconstructions in the monomodel and certain parts of the polymodal neurons in the visual cortex.
Zh Nevropatol Psikhiatr Im S S Korsakova 1976 Dec
PMID:[Several biochemical signs of loss and restoration of visual function]. 101 17

When malic enzyme is added to a mixture of malate-2-d, TPN, CO2, pyruvate, and TPNH at concentrations calculated to be at equilibrium, the TPNH level first drops and then increases slowly to its original level. This equilibrium perturbation is caused by slower cleavage of C-D than C-H bonds during hydride transfer as malate-2-d and TPNH are partly converted into TPND and malate-2-h in the process of establishing isotopic equilibrium. With malate-2-d, isotope effects for malic enzyme at pH 7.1 and malate dehydrogenase at pH 9.3 of 1.45 and 1.70-2.16 (depending on oxaloacetate level) were determined with this method, while the corresponding isotope effects on V/Kmalate and V for the chemical reactions were 1.5-1.8 and 1.0, and 1.9 and 1.5 for the two enzymes. The advantage of this method is its extreme sensitivity, and the lack of interference from various artifacts. The sensitivity is sufficient to permit determination of 13C and 15N isotope effects in favorable cases, and values of 1.031 for malic enzyme with 13CO2, and 1.047 for glutamate dehydrogenase with 15NH4+ have been determined. In the course of this work it was discovered that the equilibrium constants for oxidation by DPN, and oxidative decarboxylation by TPN are lower for malate-2-d than for malate-2-h by a factor of 0.76-0.82. Changes in Keq upon deuterium substitution, which are predicted by the calculations of Hartshorn and Shiner (1972), should be observed for many other reactions as well.
Biochemistry 1975 Dec 02
PMID:Equilibrium perturbation by isotope substitution. 119 42

The subcellular localizations of gamma-aminobutyrate transaminase (EC 2.6.1.19) and glutamate dehydrogenase (EC 1.4.1.2) in brain tissue of adult rats were compared with each other and with those of NAD+-isocitrate dehydrogenase (EC 1.1.41) and monoamine oxidase (EC 1.4.3.4; kynuramine as substrate). Crude mitochondrial fractions from brain tissue were centrifuged in continuous sucrose density gradients. gamma-Aminobutyrate transaminase and glutamate dehydrogenase were always found at a higher density than NAD+-isocitrate dehydrogenase and monoamine oxidase. When centrifuged for 1 h at 53 000gav., there was a slight difference between the distribution profiles of glutamate dehydrogenase and gamma-aminobutyrate transaminase. This difference was larger when the centrifugation time was only 15 min. It is concluded that there are subpopulations of brain mitochondria with differing proportions of gamma-aminobutyrate transaminase and glutamate dehydrogenase. The results are discussed in relation to evidence obtained with labelled precursors in vivo that there are at least two small glutamate compartments in adult brain.
Biochem J 1975 Dec
PMID:Subcellular localization of gamma-aminobutyrate transaminase and glutamate dehydrogenase in adult rat brain. Evidence for at least two small glutamate compartments in brain. 122 1

The isoenzymatic pattern of glutamate dehydrogenase (GDH) has been described for Ascaris suum a parasite of Sus scrofa domestica. Only one band of activity has been revealed, suggesting a monomorphic condition for this enzyme. Also, the structure of GDH has been assayed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and silver staining. Only one subunit was present with a molecular weight of about 55,000. A hexameric structure for GDH of A. suum is suggested.
J Helminthol 1992 Dec
PMID:Isoenzymatic pattern and structure of glutamate dehydrogenase from Ascaris suum. 129 99

Ammonia, lactate and glutamate levels and the activities of glutamine synthetase (GS), glutamate dehydrogenase (GDH), glutaminase (GLN), aspartate transaminase (AST), phosphofructokinase (PFK) and monoamine oxidase (MAO) were compared in the brain tissue of normal and P. yoelii infected mice. The brain lactate increased by 96% at peak parasitaemia. Cerebral ammonia also exhibited an increase in infected mice which was parasitaemia dependent, while glutamate remained almost unchanged. The brain glutamine synthetase registered an increase of 35% (P < 0.001) in post-mitochondrial fractions, this effect being perceptible even at low parasitaemia, but attained constancy at parasitaemia levels higher than 20%. The activity of monoamine oxidase and phosphofructokinase increased by 105% (P < 0.02) and 41% (P < 0.05) respectively while glutamate dehydrogenase decreased by 15% (P < 0.001). Glutaminase and aspartate transaminase were not significantly influenced by infection (tested only at high parasitaemia levels). It has been postulated that cerebral hypoxia and aberrations in ammonia metabolism may both contribute towards malaria induced cerebral complications.
J Trop Med Hyg 1992 Dec
PMID:Cerebral ammonia levels and enzyme changes during Plasmodium yoelii infection in mice. 136 Oct 9

The effect of gentamicin on both glutamate synthesis and glutamate deamination was studied in kidney-cortex mitochondria and tubules isolated from both control and gentamicin-treated animals. In kidney-cortex mitochondria which were permeabilized in order to make a free access of substrates and antibiotic to the glutamate dehydrogenase, gentamicin appeared to be a very potent inhibitor of glutamate synthesis, resulting in about 60% decrease of the enzyme activity at 5 mM concentration. Other aminoglycoside antibiotics decreased the enzymatic activity, in the following order: gentamicin > neomycin = tobramycin = kanamycin > biodacyna > amikacin > streptomycin. This, in principle, corresponds to their known nephrotoxic potential observed in vivo. The inhibitory action of antibiotics was abolished by neither ADP nor leucine, allosteric activators of glutamate dehydrogenase. Surprisingly, gentamicin did not decrease the rate of ammonia formation from glutamate when added to both renal tubules and mitochondria isolated from control rabbits. This indicates that the antibiotic exerts its inhibitory effect on glutamate dehydrogenase activity in the direction of glutamate synthesis only. In contrast, the rate of both glutamate deamination and glutamate synthesis was about 40% lower in renal tubules and mitochondria isolated from kidney-cortex of animals which were given antibiotics for 10 days. In view of these results it seems that (i) the depression of ammoniagenesis in gentamicin-treated animals may be due to a decrease of glutamate dehydrogenase content and (ii) under conditions in vitro the aminoglycoside inhibits the enzyme activity in the direction of glutamate synthesis while it does not affect the glutamate deamination.
Pharmacol Res 1992 Dec
PMID:Differential in vivo and in vitro effect of gentamicin on glutamate synthesis and glutamate deamination in rabbit kidney-cortex tubules and mitochondria. 136 90

The hepatotoxicity and the relationship between the hepatotoxicity and free radical induced by 1,1,2-trichloroethane (1,1,2-TCE) and 1,1,1-trichloroethane (1,1,1-TCE) were studied by whole animals test and the isolated perfused rat liver test. Enzymatic parameters measured during the test included the assay of levels of glutamic pyruvic transaminase (GPT), sorbital dehydrogenase (SDH) and glutamate dehydrogenase (GDH). The observation of the pathologic changes of the liver by the light microscope and the measurement of the relative total free radical concentration in the liver were also made. The results showed that 1,1,2-TCE caused definite pathologic changes of rat liver. It led to much higher values for GPT, SDH and GDH both in serum and perfusate than 1,1,1-TCE did (P < 0.01). The concentration of perfusate K+ caused by 1,1,2-TCE was higher than that by 1,1,1-TCE (P < 0.01). The value of the relative total free radical concentration induced by 1,1,2-TCE was also greater than that by 1,1,1-TCE (P < 0.05). The results suggested that the hepatotoxicity of 1,1,2-TCE was stronger than that of 1,1,1-TCE. The free radical concentration was increased proportionally to the increase of the hepatotoxicity of 1,1,2-TCE and 1,1,1-TCE. It appeared that free radical may play an important role in the mechanism of the hepatic injury induced by 1,1,2-TCE.
Biomed Environ Sci 1992 Dec
PMID:Study of the relationship between the hepatotoxicity and free radical induced by 1,1,2-trichloroethane and 1,1,1-trichloroethane in rat. 148 24

Microsome, cytosol and serum malathion carboxylesterase (MaCEst) activity was assessed in rats after single i.p. administration of carbon tetrachloride (CCl4) in doses ranging from 0.05 to 1 ml kg-1. MaCEst activities were compared with those of glucose-6-phosphatase (G6-Pase) as an indicator of endoplasmic reticulum damage and serum glutamate dehydrogenase (GLDH) and sorbitol dehydrogenase (SHD) as indicators of liver cytolysis. The data showed a dose-dependent increase in GLDH and SDH serum activities (175% and 68%) from 0.05 ml kg-1; an increase in serum G6-Pase (31%) and a decrease in microsomal G6-Pase (38%) was apparent only after 0.5 or 1.0 ml kg-1 doses. MaCEst activity was unaffected. The results demonstrate that, under these experimental conditions, serum and subcellular measurements of MaCEst activity failed to reveal the liver toxicity of CCl4.
J Appl Toxicol 1991 Dec
PMID:Difference in liver and serum malathion carboxylesterase and glucose-6-phosphatase in detecting carbon tetrachloride-induced liver damage in rats. 166 44

We analyzed the upstream region of the GDH2 gene, which encodes the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae, for elements important for the regulation of the gene by the nitrogen source. The levels of this enzyme are high in cells grown with glutamate as the sole source of nitrogen and low in cells grown with glutamine or ammonium. We found that this regulation occurs at the level of transcription and that a total of six sites are required to cause a CYC1-lacZ fusion to the GDH2 gene to be regulated in the same manner as the NAD-linked glutamate dehydrogenase. Two sites behaved as upstream activation sites (UASs). The remaining four sites were found to block the effects of the two UASs in such a way that the GDH2-CYC1-lacZ fusion was not expressed unless the cells containing it were grown under conditions favorable for the activity of both UASs. This complex regulatory system appears to account for the fact that GDH2 expression is exquisitely sensitive to glutamine, whereas the expression of GLN1, coding for glutamine synthetase, is not nearly as sensitive.
Mol Cell Biol 1991 Dec
PMID:Role of the complex upstream region of the GDH2 gene in nitrogen regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae. 168 1


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