Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Suspensions of enzymatically prepared hepatocytes from starved rats were separated according to their buoyant density at 12 degrees C in linear, isosmotic gradients of metrizamide, centrofuged at low speed for a relatively short time. The recovery of cell protein was 86%. Hepatocytes of high viability formed a single band around 1.10 g/cm3 and were recovered as four density populations (P1-P4) form low to high density, respectively. The content of protein was significantly lower in population P1, while the content of neutral fat or the averaged cell size was similar in the various populations. The specific activity of alanine aminotransferase increased in the order P1-P4. The distribution of this enzyme within the intact liver acinus obtained by others indicate that a partial separation of periportal and perivenous hepatocytes had occurred. The activity patterns of lactate dehydrogenase, glutamate dehydrogenase, isocitrate dehydrogenase (NADP+) and pyruvate kinase, also with known intra acinar distributions, supported this conclusion. The hepatocytes showed signs of shrinkage after separation, but since they retained a normal ultrastructure, most enzyme activities and viability, the present technique was regarded superior to previous procedures of hepatocyte separation by density. The degree of separation was calculated from an equation (see Appendix), and the periportal/perivenous ratio for parameters measured in density populations can be obtained. The specific activity of phosphofructokinase, alcohol dehydrogenase and aldehyde dehydrogenase showed no differences between populations. However, the ratio high-Km/low-Km aldehyde dehydrogenase increased in the order P4-P1.
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PMID:Partial separation and biochemical characteristics of periportal and perivenous hepatocytes from rat liver. 702 82

1. The maximum activity of hexokinase in lymphocytes is similar to that of 6-phosphofructokinase, but considerably greater than that of phosphorylase, suggesting that glucose rather than glycogen is the major carbohydrate fuel for these cells. Starvation increased slightly the activities of some of the glycolytic enzymes. A local immunological challenge in vivo (a graft-versus-host reaction) increased the activities of hexokinase, 6-phosphofructokinase, pyruvate kinase and lactate dehydrogenase, confirming the importance of the glycolytic pathway in cell division. 2. The activities of the ketone-body-utilizing enzymes were lower than those of hexokinase or 6-phosphofructokinase, unlike in muscle and brain, and were not affected by starvation. It is suggested that the ketone bodies will not provide a quantitatively important alternative fuel to glucose in lymphocytes. 3. Of the enzymes of the tricarboxylic acid cycle whose activities were measured, that of oxoglutarate dehydrogenase was the lowest, yet its activity (about 4.0mumol/min per g dry wt. at 37 degrees C) was considerably greater than the flux through the cycle (0.5mumol/min per g calculated from oxygen consumption by incubated lymphocytes). The activity was decreased by starvation, but that of citrate synthase was increased by the local immunological challenge in vivo. It is suggested that the rate of the cycle would increase towards the capacity indicated by oxoglutarate dehydrogenase in proliferating lymphocytes. 4. Enzymes possibly involved in the pathway of glutamine oxidation were measured in lymphocytes, which suggests that an aminotransferase reaction(s) (probably aspartate aminotransferase) is important in the conversion of glutamate into oxoglutarate rather than glutamate dehydrogenase, and that the maximum activity of glutaminase is markedly in excess of the rate of glutamine utilization by incubated lymphocytes. The activity of glutaminase is increased by both starvation and the local immunological challenge in vivo. This last finding suggests that metabolism of glutamine via glutaminase is important in proliferating lymphocytes.
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PMID:Maximum activities of some enzymes of glycolysis, the tricarboxylic acid cycle and ketone-body and glutamine utilization pathways in lymphocytes of the rat. 716 29

The activities of 13 liver and 6 brain enzymes were studied in 7-12 week old CD2F1 male mice that had been fed ad libitum and standardized either to 12 hours of light (0600-1800) alternating with 12 hours of darkness (1800-0600) (LD12:12); or to a reversed light-dark cycle (darkness 0600-1800; light 1800-0600) (DL12:12). Three separate studies were performed on two different days; in each experiment, subgroups of 14 animals were sacrificed at 3-hour intervals. Livers were assayed for: isocitrate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase, glutathione reductase, glyoxylate reductase, L-alanine aminotransferase, glutamate oxalacetate transaminase, pyruvate decarboxylase, fructose-1-phosphate aldolase, fructose diphosphate aldolase, fructose 1,6-diphosphatase, and fatty acid synthetase. Brains were assayed for phosphoglucose isomerase, adenosine triphosphatase, creatine phosphokinase, pyruvate kinase, adenylate kinase, and malate dehydrogenase. All 19 enzymes demonstrated a prominent circadian rhythm in at least one experiment. Moreover, each rhythmic variable showed a statistically significant fit to a 24-hour cosine (sine) curve by the method of least squares. In general, peak activities of the liver enzymes analyzed were associated with the beginning of the dark cycle and initiation of the animal's activity, while the group of brain enzymes had peak activities which occurred at the beginning of the animals' rest span and were near the beginning of the light cycle. The phasing of each of the rhythms could be reversed within a two-week span after reversing the environmental light-dark cycle 180 degrees.
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PMID:Circadian organization of thirteen liver and six brain enzymes of the mouse. 731 49

Male weanling rats were meal-fed (2 hours daily) on a vitamin B-6-deficient diet for 8 weeks; the controls were pair-fed. Vitamin B-6 deficiency led to the expected decreases in the activities of hepatic alanine and aspartate aminotransferases but did not influence those of glutamate dehydrogenase (EC 1.4.1.2), pyruvate carboxylase (EC 6.6.1.1), phosphoenolpyruvate carboxykinase (EC 4.1.1.32) and pyruvate kinase (EC 2.7.1.40). The ability of the deficient rats to incorporate 14C from labeled alanine into blood glucose and expired CO2 was diminished, but pyruvate-U-14C was utilized normally. The deficiency did not influence gluconeogenesis from glutamate or 2-oxoglutarate. Furthermore, the gluconeogenic potential of renal cortex slices incubated with pyruvate or 2-oxoglutarate was unaltered by the deficiency. These data suggest that the impairment of gluconeogenesis from amino acids in vitamin B-6 deficiency may be the consequence of diminished transamination prior to oxidative deamination.
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PMID:Gluconeogenesis in meal-fed, vitamin B-6-deficient rats. 735 97

Alveolar and peritoneal macrophages differ in their energy metabolism. Alveolar macrophages are mainly aerobic whereas peritoneal macrophages are mainly anaerobic in their energy generation. We investigated the question of whether these differences in metabolism are preprogrammed in subsets of macrophage precursors in the bone marrow, or develop in proliferating cells as a consequence of exposure to different tissue environments. The progeny of single mouse macrophage progenitor cells were grown in vitro for 4 days; the resultant colonies were divided into two roughly equal populations, which were cultured in either a high or low oxygen environment corresponding to that of the alveoli or tissues. Following 4 days incubation at 5% or 20% O2, the activities of the two glycolytic enzymes lactate dehydrogenase (LDH) and pyruvate kinase (PK) were two- to threefold higher in the half of the colonies grown in the low O2 environment, whereas the activity of the oxidative phosphorylative enzyme glutamate dehydrogenase (GDH) was two- to threefold higher in the half colony grown in the aerobic environment. Re-exposure of the cells from the low O2 environment to high O2 conditions for an additional 4 days caused a rise in the GDH activity and a decrease in the LDH and PK. The recovery of the GDH activity after the re-exposure was time dependent. Our results support the theory that macrophages arising from a single progenitor cell can develop different metabolic features depending on the O2 environment in which they mature. A single precursor cell can give rise to mature cells with metabolic characteristic of either alveolar or tissue macrophages.
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PMID:The progeny of a single progenitor cell can develop characteristics of either a tissue or an alveolar macrophage. 744 18

The activity and some kinetic parameters of the key enzymes of the glycolysis, the gluconeogenesis and the amino acid catabolism from the liver of male and female mink have been determined and compared to the corresponding activities from rat and cat. The activities of glucose-6-phosphatase and pyruvate kinase are dependent on sex, both being higher in females. Except for pyruvate carboxylase the glycolytic and the gluconeogenic enzyme activities of the mink are higher than those of rat and cat; especially the activities of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase are markedly higher. The activities of glutamate dehydrogenase and glutamate oxaloacetate transaminase are smaller than the corresponding activities of rat but higher than those of cat. The results suggest that mink has a high capacity for gluconeogenesis compared to rat.
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PMID:Activities of carbohydrate and amino acid metabolizing enzymes from liver of mink (Mustela vison) and preliminary observations on steady state kinetics of the enzymes. 758 47

Freshly isolated viable rat hepatocytes were separated into five subpopulations on shallow discontinuous Percoll density gradients. The periportal marker enzymes alanine aminotransferase (ALT), malate dehydrogenase (MDH) and lactate dehydrogenase (LDH) showed gradients of increasing activity from the subpopulation of least density (band 1, rho = 1.07 g/ml) to the subpopulation of greatest density (band 5, rho = 1.09 g/ml). The perivenous marker enzymes pyruvate kinase (PK) and glutamate dehydrogenase (GDH) showed gradients of decreasing activity from band-1 cells to band-5 cells. Glutamine synthetase (GS), which is confined to the two or three cell layers around the hepatic venule, was almost entirely restricted to band-1 hepatocytes. Band-5: band-1 ratios of enzyme activity were as follows: ALT, 8.0; LDH, 2.1; MDH, 1.6; GDH, 0.7; PK, 0.2; GS, 0.01. Band-5:band-1 ratios for ALT, LDH, PK and GS were maintained after culture of subpopulations in identical conditions for up to 72 h, whereas the ratios for MDH and GDH decreased and increased respectively towards unity. Band-1 hepatocytes exhibited greater cytotoxicity than band-5 cells after incubation with carbon tetrachloride or paracetamol. These perivenous-selective toxins produced greater decreases in cell viability and greater release of ALT and LDH from band-1 hepatocytes than from band-5 hepatocytes. Conversely, band-5 hepatocytes were more susceptible than band-1 hepatocytes to the cytotoxic effects of 1-naphthylisothiocyanate and methotrexate (known periportal-selective toxins). It is concluded that band-5 hepatocytes are enriched in periportal cells, whereas band-1 hepatocytes are enriched in perivenous cells. Isolation of hepatocyte subpopulations by Percoll density-gradient centrifugation has the considerable advantage that periportal and perivenous cells can be obtained from the same liver.
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PMID:Subpopulations of rat hepatocytes separated by Percoll density-gradient centrifugation show characteristics consistent with different acinar locations. 799 99

The effects of urea, cations (K+,NH4,Na+,Cs+,Li+), and trimethylamines on the maximal activities and kinetic properties of pyruvate kinase (PK) and phosphofructokinase (PFK) from skeletal muscle were analyzed in two anuran amphibians, an estivating species, the spadefoot toad Scaphiopus couchii, and a semi-aquatic species, the leopard frog Rana pipiens. Urea, which accumulates naturally to levels of 200-300 mM during estivation in toads, had only minor effects on the Vmax, kinetic constants and pH curves of PK from either species and no effects on PFK Vmax or kinetic constants. Trimethylamine oxide neither affected enzyme activity directly or changed enzyme response to urea. By contrast, high KCl (200 mM) lowered the Vmax of toad PFK and of PK from both species and altered the Km values for both substrates of frog PFK. Other cations were even more inhibitory; for example, the Vmax of PK from either species was reduced by more than 80% by the addition of 200 mM NH4Cl, NaCl, CsCi, or LiCl. High KCl also significantly changed the Km values for substrates of toad lactate dehydrogenase and strongly reduced the Vmax of glutamate dehydrogenase and NAD-dependent isocitrate dehydrogenase in both species whereas 300 mM urea had relatively little effect on these enzymes. The perturbing effect of urea on enzymes and the counteracting effect of trimethylamines that has been reported for elasmobranch fishes (that maintain high concentrations of both solutes naturally) does not appear to apply to amphibian enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Urea and salt effects on enzymes from estivating and non-estivating amphibians. 804 69

There are several advantages to the use of progress curves to analyze the the kinetic properties of enzymes but most studies still rely on rate measurements. One of the reasons for this may be that progress curve analysis relies on the enzyme and the reactants being completely stable under assay conditions. Here a method is described that relaxes this requirement and allows progress curve analysis to be applied to unstable enzymes. The procedure is based on a combination of numerical integration and non-linear regression to fit rate equations to the progress curve data. The analysis is verified using simulated data and illustrated by application to the reaction catalyzed by alkaline phosphatase, measured in the presence of 10 mM EGTA where it has a half-life of 3 1/2 min. The method may also be applied to other experimental systems where the development over time reveals important properties but where an analytical solution of the underlying model is not known. This extension is illustrated by two systems: the coupled reactions catalyzed by pyruvate kinase and lactate dehydrogenase under conditions where both enzymes have similar activity; and the transient-state kinetics of the reaction catalyzed by glutamate dehydrogenase.
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PMID:Analysis of progress curves for enzyme-catalyzed reactions: application to unstable enzymes, coupled reactions and transient-state kinetics. 815 8

Efficient energy utilization is essential for cell growth; in an attempt to improve the growth conditions of the rat T-lymphocyte culture model for potential use in studying the mutagenic activity of carcinogens in vitro, we have investigated the effects of phytohemagglutinin (PHA), interleukin-2 (IL-2) and 2-mercaptoethanol (2-ME) on the activities of intermediary metabolism enzymes and cell proliferation. Isolated lymphocytes were cultured in the presence and absence of PHA, IL-2, or 2-ME. The intermediary metabolism enzymes investigated were glutamate dehydrogenase, glutamate-pyruvate transaminase, malate dehydrogenase, isocitrate dehydrogenase, lactate dehydrogenase, pyruvate kinase, and fatty acid synthetase (FAS). Measurable activity of all enzymes investigated, except for FAS, was detected in PHA-stimulated cells cultured with IL-2 or 2-ME. The unstimulated lymphocytes had significantly lower enzyme activity than stimulated cells. The combination of all three agents showed increased enzyme activity. This increase in activity brought about by the combination of the three agents was not reproduced by either agent acting alone. In general, the increase in enzyme activity correlated with cell proliferation as measured by [3H]thymidine uptake in PHA-stimulated cultures containing IL-2 and/or 2-ME. The results suggest that the addition of exogenous IL-2 and 2-ME enhances metabolic function and may be beneficial in in vitro culture of rat lymphocytes.
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PMID:Characterization of rat lymphocyte primary culture for the development of an in-vitro mutagenesis assay: effect of interleukin-2 and 2-mercaptoethanol on the activities of intermediary metabolism enzymes and cell proliferation. 873 77


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