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)

The activities of eight enzymes (glutamate dehydrogenase, sorbital dehydrogenase, malate dehydrogenase, lactate dehydrogenase, alpha-hydroxy butyrate dehydrogenase, gamma-glutamyl transpeptidase, alkaline phosphatase and creatine kinase) were determined in tissue homogenates of liver, kidney, spleen, lung, small intestine, cardiac muscle and skeletal muscle, from 15 Large White pigs of three different ages (1.5 weeks, 18--22 weeks and 113 weeks). The results showed that variation in tissue enzyme concentration due to differences in sex is minimal. Variation due to differences in age, however, appears to be of greater importance, particularly when considering young animals. These age differences may affect the interpretation of plasma enzyme changes due to tissue damage, and the use of additional enzyme assays as an aid to interpretation in these cases is advisable.
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PMID:Enzyme activities in tissues of clinically normal Large White pigs. Variations with age and sex. 60 99

In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, 'nothing dehydrogenase' reaction, use of exogenous CoQ10 and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of L-glutamate dehydrogenase (E.C.1.4.1.2 and E.C.1.4.1.3) have been investigated in the rat cerebellum. It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ10, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type. Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.
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PMID:Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. 66 87

Twenty experiments were conducted on dogs. The effect of hypothermia of different degree (from 18 to 20 degrees C and from 4 to 6 degrees C) on the carbohydrate metabolism and the extent of solubilization of hepatic enzymes (lactate dehydrogenase, glutamate dehydrogenase, urokaninase, DNA-ase, glucose-6-phosphatase) in prefusion-free preservation of the liver was studied. The preservation efficacy was assessed during the subsequent two-hour normothermic perfusion. A marked solubilization of the enzymes under study followed preservation of the liver at 18--20 degrees C; this indicated the loss of intactness of the cell membranes during the preservation. A moderate expenditure of the glycogen stores in the liver, and of sugar in the perfusate followed preservation of the liver at a temperature of 4--6 degrees C; this suggested an even suppression of hepatic metabolism and the prevalence of normal tissue respiration over glycolysis in the restoration of circulation in the liver.
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PMID:[Effect of hypothermia on metabolism in the liver during its preservation]. 68 13

In experimental investigations on Eimeria stiedai infected rabbits, serum enzymatic studies have been carried out in correlation with the examination of parasitological and pathological parameters. The rabbits were orally infected with a single dose of either 100,000 or 250,000 sporulated oocysts. Increase of the activity of the sorbit dehydrogenase (SDH), glutamate oxalate transaminase (GOT), glutamate pyruvate transaminase (GPT) and glutamate dehydrogenase (GlDH) could be found first between 3 and 10 days after infection indicating the beginning of the acute phase of liver coccidiosis. The increase of the conjugated bilirubin and of the gamma-glutamyl-transferase (gamma-GT) could be found not earlier than 10 days after infection and is to be explained as sign of disturbed efficiency of excretion. The various investigated parameters reached their peak of alteration about the end of the prepatent period and at the beginning of patency between 14 and 21 days after infection. The results emphasize the value and usefulness of serum enzymes, particularly the glutamate dehydrogenase (GlDH) and the gamma-glutamyl-transferase (gamma-GT) with about 30fold activity, as indicators in the course of Eimeria stiedai infection of rabbits. The enzymes returned to physiological values at the end of the experiment, 42 days after infection. Significant differences could not be detected within the infected groups. The activities of the alkaline phosphatase (AP), leucine aminopeptidase (LAP), choline esterase (ChE), lactate dehydrogenase (LDH) and isoenzym 1 (alpha-HBDH) showed only slight alterations and proved to be no significant parameters for the pathophysiological evaluation of the liver coccidiosis.
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PMID:[Alteration of enzyme activities in serum of Eimeria stiedai infected rabbits (author's transl)]. 73 5

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52

Twenty calves were infected with 1000 metacercariae of Fasciola hepatica, the activities of 10 enzymes in plasma or serum were assayed and concentrations in serum of proteins, urea and bilirubin were determined. These values were compared with control data obtained from 14 uninfected calves. Aspartate aminotransferase, lactate dehydrogenase, sorbitol dehydrogenase, glutamate dehydrogenase, ornithine carbamoyl transferase and gamma-glutamyl transpeptidase activities increased in infected calves. Total serum protein increased, albumin decreased, globulin increased and the albumin/globulin ratio was decreased in infected calves. Plasma alanine aminotransferase, leucine aminopeptidase, alkaline phosphatase and cholinesterase activities and serum concentration of urea and bilirubin were unaffected. It was concluded that glutamate dehydrogenase and gamma-glutamyl transpeptidase were the most sensitive indicators of liver cell damage in fascioliasis.
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PMID:Biochemical indicators of liver injury in calves with experimental fascioliasis. 83 11

Changes in serum enzyme levels, liver histology and liver function tests have been correlated to determine the usefulness of these tests in assessing liver status. The effects of carbon tetrachloride administration on these parameters has been determined in a group of 20 sheep. Normal levels, elevated levels after injury and the effect of elapsed time after injury are reported for serum glutamic dehydrogenase, sorbitol dehydrogenase, glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, lactate dehydrogenase, fructose-1-phosphate adlolase, alkaline phosphatase, cholesterol and proteins. Variation in the time of elevation of enzyme activities may be useful in determining the elapsed time between acute injury and serum sampling. In comparison to sheep fed an adequate diet, a diet with a restricted protein intake was associated with increased severity of histological lesions and decreased liver function.
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PMID:A comparison of parameters used to assess liver damage in sheep treated with carbon tetrachloride. 92 59

The method for the determination of enzymic activity in turbid, lipaemic sera, which involves clearing by polyanion precipitation with heparin and magnesium chloride, was critically reviewed. In the diagnosis of diseases of the liver and pancreas, which are frequently associated with hyperlipoproteinaemia, only residual enzyme activities are measured in the cleared serum after polyanion treatment. In the measurement of glutamate dehydrogenase and in the Phadebas test for alpha-amylase, the enzymes are inactivated by treatment with heparin and magnesium chloride. On the other hand, as a result of polyanion precipitation gamma-glutamyl transferase is transferred, together with lipoproteins and chylomicrons, to the lipid-rich supernatant. Acid phosphatase also exhibits only residual activity in cleared serum. The activity of aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, leucine arylamidase, cholinesterase, creatine kinase, lactate dehydrogenase, and alpha-hydroxybutyrate dehydrogenase, and the activity of alpha-amylase in the Merckotest are not affected by polyanion treatment of the serum.
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PMID:[Enzyme diagnosis in lipaemic sera before and after polyanion precipitation with heparin and magnesium chloride (author's transl)]. 92 35

The occurrence and levels of activity of various enzymes of carbohydrate catabolism in culture forms (promastigotes) of 4 human species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, and L. tropica) were compared. These organisms possess enzymes of the Embden-Meyerhof pathway but lack lactate dehydrogenase. No evidence could be found for the production of lactic acid by growing cultures and lactic acid could not be detected either in cell-free preparations or after incubation of cell-free extracts with pyruvate and NADH under appropriate conditions. All 4 species possess alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate phosphatase which together could regenerate NAD, thus compensating for the absence of lactate dehydrogenase. The oxidative and nonoxidative reactions of the hexose monophosphate pathway are present in all 4 species. Cell-free extracts have pyruvate dehydrogenase activity which allows the entry of pyruvate into and its subsequent oxidation through the tricarboxylic acid cycle. All enzymes of this cycle, including a thiamine pyrophosphate dependent alpha-ketoglutarate dehydrogenase, are present. Both NAD and NADP-linked malate dehydrogenase activities are present. The isocitrate dehydrogenase is NADP specific. There is an active glutamate dehydrogenase which could compete with alpha-ketoglutarate dehydrogenase for the common substrate (alpha-ketoglutarate). Replenishment of C4 acids is accomplished by heterotrophic CO2 fixation catalyzed by pyruvate carboxylase. All 4 species have high levels of NADH oxidase activity. Several enzymes thus far not found in any species of Leishmania have been demonstrated. These are: phosphoglucose isomerase, triose phosphate isomerase, fructose-1, 6-diphosphatase, 3-phosphoglycerate kinase, enolase, alpha-glycerophosphate dehydrogenase, alpha-glycerophosphate phosphatase, pyruvate dehydrogenase complex, citrate synthase, aconitase, alpha-ketoglutarate dehydrogenase, glutamate dehydrogenase, and NADH oxidase.
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PMID:Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative survey. 100 46

The adsorption of 8 enzymes to polyaminomethylstyrene was studied. While lactate dehydrogenase, alkaline phosphatase and glucose-6-phosphate dehydrogenase exhibit a relatively low affinity to the carrier, alcohol dehydrogenase, glutamate dehydrogenase and urease were found to form stabile complexes with the polymer that are enzymatically active. Adsorbed urease and beta-hydroxybutyrate dehydrogenase, are still active after several weeks; the other preparations lose their activity soon. It can be shown by the example of yeast alcohol dehydrogenase that the activity loss following adsorption is caused possibly by a process of reorientation of already bound enzyme molecules or by the increasing enzyme coverage of the carrier, with the active centres becoming more and more inaccessible for the substrate. During the substrate conversion catalysed by the alcohol dehydrogenase-polyaminomethylstyrene complex, a small amount of the enzyme is again detached from the carrier. The activity rises to a certain extent in the supernatant but drops to zero again. The stability of the adsorbed urease is distinctly increased compared with the dissolved enzyme. For the pH optimum and the KM value there are no differences between the two preparations. Continuous application of polyaminomethylstyrene-bound beta-hydroxybutyrate dehydrogenase and urease, respectively, in a column shows that both preparations have unchanged enzymatic activities even after running times of 5 and 24 days, respectively.
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PMID:[Kinetic properties of enzymes in particular of yeast alcohol dehydrogenase following their adsorption on polyaminomethylstyrene]. 102 29


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