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 different doses of chlorfenvinphos given in diets with low-protein and optimal-protein level to young Wistar rats of both sexes were, after 10 or 30 days, without the significant influence on the activity of several serum enzymes used as diagnostic markers in determining the liver damage or disease, as for example:sorbitol dehydrogenase, glutamic dehydrogenase, glucosephosphate isomerase (PHI), aspartate and alanine aminotransferase. Not even important changes were found in the activity of aromatic amino acids aminotransferases in the brain and in protein content in the brain and liver of rats fed diets contaminated with chlorfenvinphos, irrespective of the protein concentration in the diet. Only in some cases at the highest concentration of chlorfenvinphos in the diets the decreased activity of aromatic amino acids aminotransferases appeared in the liver, more evident in low-protein rats. The decrease of the PHI activity in the brain and the inhibition of acetylcholinesterase activity in the serum and brain depended mainly on the amount of chlorfenvinphos in the diets and to a lower degree on the amount of protein. All changes caused by chlorfenvinphos normalized during two weeks after its elimination from the diets.
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PMID:Alterations in some biochemical processes in the organism of rats being under the influence of chlorfenvinphos administered in diets with variable protein content. 648 45

Glutamic dehydrogenase (GDH) activity in rat heart was found to be 2.1 U/g of heart (wet wt). The mitochondrial glutamic dehydrogenase activity accounted for only 18% of the total. This percentage of the total activity in heart mitochondria was not altered by nagarse treatment, acetone extraction, sonication in Triton X-100, and extraction with buffer containing a protease inhibitor. The remainder of the activity was present in the cytosol. Cytosolic GDH activity differed from mitochondrial GDH activity by its pH curve, stability to heat, Arrhenius plot, and the effect of different nucleotides. Acetone extraction of the mitochondria resulted in GDH that was stable to heat and had a shallow temperature activation curve resembling cytosolic GDH. Acetone extraction of cytosolic GDH inactivated it. The cytosolic activity was purified 288-fold and the mitochondrial activity 100-fold. Purified cytosolic and mitochondrial GDH enzymes had different monomeric molecular weights on sucrose density gradient centrifugation. Gel filtration of cytosolic and mitochondrial GDH also showed different monomeric molecular weights. We conclude that rat heart GDH exists in two forms with different physical and kinetic characteristics. The majority of GDH activity in rat heart is cytosolic. The mitochondrial enzyme has a lipid-soluble component that can be removed with acetone without destroying its activity.
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PMID:Glutamic dehydrogenase activity in rat heart: demonstration of two forms of enzyme activity. 672 Sep 7

Glutamic dehydrogenase extracted with tris buffer from fresh freeze-thawed rat heart mitochondria was purified by ammonium sulphate fractionation, affinity chromatography on GTP agarose, hydroxyapatite chromatography and concentration using a molecular sieve. The final specific activity is 80 units/mg protein. Thin gel SDS electrophoresis of the purified enzyme preparation after reduction with dithiothreitol shows a major band with a molecular weight of 38 000 Daltons. Two minor bands are also present. Sucrose density gradient centrifugation reveals a molecular weight of 230 000 Daltons for unreduced mitochondrial GDH activity. By gel filtration rat heart mitochondrial glutamic dehydrogenase has a major peak at 230 000 Daltons, a minor peak at 300 000 Daltons and some larger molecular weight species. Rat liver mitochondrial glutamic dehydrogenase has a minor peak at 230 000, a major peak at 300 000 and some larger molecular weight species. The rat liver mitochondrial glutamic dehydrogenase predominance at 300 000 is unchanged by incubation, extraction and purification with rat heart mitochondria. The purified GDH is stable frozen at -10 degrees C in tris-HCl buffer with EDTA. It loses activity at 4 degrees C especially when stored in 0.2 M phosphate buffer. It also loses activity when dialyzed for 24 h. This loss of activity is not completely prevented by adding nucleotides to the buffer (AMP or ADP) but is decreased by their presence.
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PMID:Glutamic dehydrogenase from rat heart mitochondria. I. Purification and physical properties including molecular weight determination. 672 19

Glutamic dehydrogenase purified from rat heart mitochondria has been characterized with regard to its substrate kinetics and the influence of nucleotides and potassium phosphate on its kinetic properties. The enzyme had characteristics similar to liver mitochondrial glutamic dehydrogenase. These included several double reciprocal plots which were biphasic, indicating homotropic interaction; inhibition by GTP, which was overcome by ADP and phosphate; and activity with both NAD(H) and NADP(H). There were a number of significant differences however, in the specific kinetic properties of heart mitochondrial glutamic dehydrogenase. The Vmax of reductive amination was four-fold greater with NADH than with NADPH. The maximum rate of oxidative deamination was ten-fold greater with NAD compared to NADP. The differences also included: saturating levels of NADH and NADPH were stimulatory rather than inhibitory; ammonia was stimulatory at millimolar levels; NADP and alpha-ketoglutarate were both inhibitory at saturating levels; and ADP increased reductive amination 30% at lower levels of NADH but inhibited at higher (stimulatory) levels of NADH.
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PMID:Glutamic dehydrogenase from rat heart mitochondria. II. Kinetic characteristics. 672 20

Stereologic ultrastructural methods were applied to several cell types involved in the production of monoclonal antibodies against the mitochondrial enzyme glutamic dehydrogenase (GDH). These cell types included SP2/O murine cells, in vitro cultured hybrid cells producing monoclonal antibodies, and the same hybrid cells maintained as solid and ascites tumors (TH and ATH cells, respectively). The statistical analysis of quantitative data indicates that the fusion between SP2/O cells and spleen lymphocytes does not induce significant changes in the fine structure of the former cells. Moreover, the transfer of hybrid cells from in vitro to in vivo conditions induces their transformation from an immature state to mature plasma cells. The increase in mitochondria and rough endoplasmic reticulum suggests that the ascites tumor provides cells with an environment more suitable for expressing their activity than does the solid tumor.
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PMID:Stereological study of murine myeloma and hybridoma cells in vitro and in vivo. 687 17

1. The acute oral LD50 and chronic LC50 toxicity values for ethylene dibromide (EDB) were estimated for japanese quail. 2. Single sub-acute oral and intraperitoneal doses of EDB (1/2 LD50) and chronic oral doses of EDB (1/3 LC50) were administered to quail in order to characterise the sub-lethal effects of EDB residues. 3. At 24 h after sub-acute dosing, relative liver weight, plasma aspartate aminotransferase (AT) [EC 2.6.1.1] and L-iditol (sorbitol) dehydrogenase (SDH) [EC 1.1.1.14] were elevated and decreases were found in hepatic total lipid, total protein, AT and glutamic dehydrogenase (NAD (P)+) (GDH) and plasma cholinesterase (ChE) [EC 3.1.1.8] and total lipid. 4. Following chronic administration, elevations in relative liver weight, plasma ChE and total lipid, haemoglobin and haematocrit were found and hepatic AT, GDH and total lipid were decreased. 5. The changes in hepatic and plasma enzymes and constituents are discussed in relation to possible biphasic effects resulting from EDB exposure.
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PMID:A study on the toxicity and the biochemical effects of ethylene dibromide in the Japanese quail. 702 16

Gossypol was isolated and purified from cotton seed flour. It was found to inhibit rat testis cytosolic LDH-X activity, in vitro, in a dose-dependent manner. Preincubation of the enzyme with gossypol increased the inhibitory effect markedly. Addition of NADH to the preincubation mixture imparted some protection against inhibition. The inhibitory effect of gossypol was competitive with respect to NADH, but non-competitive with respect to alpha-ketoglutarate. The latter is reported to be a specific substrate for rat LDH-X and hence can be used for measuring LDH-X activity in the presence of other lactic dehydrogenase isoenzymes. Preliminary studies show that gossypol can inhibit other dehydrogenases such as glutamic dehydrogenase, glutathione reductase and malic dehydrogenase as well.
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PMID:Inhibition of rat testis LDH-X activity by gossypol. 716 54

Compared to controls receiving physiological saline, the i.p. administration of dimethylnitrosamine (DMN) on 5 consecutive days to rats fed a nutritionally adequate liquid diet resulted 24 hours after the last injection of significant increases in glutamic dehydrogenase (GDH), glutamic oxylacetate transaminase (GOT), and glutamic pyruvate transaminase (GPT) activities in the serum, indicating a striking hepatotoxic effect of this compound. This was confirmed by the histological demonstration of massive centrolobular necrosis. Conversely, following pretreatment of the rats with an ethanol containing liquid diet for 23 days and subsequent administration of DMN the increases of serum enzyme activities and massive centrolobular necrosis could not be observed. These results therefore suggest that chronic alcohol consumption protects from hepatotoxicity due to DMN, most probably due to an enhancement of detoxifying pathways of the parent component or one of its toxic metabolites.
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PMID:Decreased hepatotoxicity of dimethylnitrosamine (DMN) following chronic alcohol consumption. 719 20

The numerous physiological and nutritional factors which influence the concentration of serum calcium are considered. The causes of hypercalcaemia and hypocalcaemia are briefly discussed, with particular reference to the clinical symptoms and pathology. The effect of the acid-base status on the serum-ionized calcium level is stressed. The causes of changes in the serum concentrations of phosphorus and magnesium are briefly reviewed, along with the abnormalities of lactate, pyruvate, and hydrogen ion concentrations. The kidney function tests, blood urea nitrogen, serum creatinine, and the renal clearance tests are discussed, with emphasis placed on correlating their results with the findings from repeated urinalyses. The important physiologic influences and pathological processes which result in changes in the concentrations of these parameters are delineated. The causes of increases in the serum enzymes, alkaline phosphatase, alanine transaminase, asparate transaminase, lactic dehydrogenase, sorbitol dehydrogenase, glutamic dehydrogenase, gamma glutamyl transpeptidase, creatinine phosphokinase, amylase and lipase are discussed. The changes in serum bilirubin concentration and its components are fully described, with emphasis placed on the correlation of the findings with urinalysis data and the complexities resulting from the numerous pathologic conditions causing jaundice. These conditions are listed for each of the domestic animals. The other liver function tests, bromosulphthalein dye retention or excretion, serum uric acid and blood ammonia concentration are briefly considered. All the tests described are very useful, and frequently essential, in aiding the veterinary practitioner to arrive at a diagnosis and prognosis, but they never replace clinical acumen.
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PMID:Correlation of changes in blood chemistry with pathological changes in the animal's body: II Electrolytes, kidney function tests, serum enzymes, and liver function tests. 727 79

The willow ptarmigan has two large caeca housing dense populations of microorganisms. Urine, containing uric acid, is transported from the cloaca into the caeca when these are filled. Here the uric acid is rapidly broken down, suggesting that the caeca take part in a recycling of excretory nitrogen. In this work it is shown that ammonia produced by the uric acid decomposition is incorporated into new amino acids in a glutamic dehydrogenase catalyzed reaction. We have, however, not been able to detect any absorption of amino acids from the caeca, indicating that nitrogen recycling via the amino acid route does not occur.
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PMID:On caecal synthesis and absorption of amino acids and their importance for nitrogen recycling in willow ptarmigan (Lagopus lagopus lagopus). 734 31


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