Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.4.3.11 (glutamate dehydrogenase)
 4,437 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of GOT, GPT, LDH, gamma-glutamyltranspeptidase (gamma-GTP), alkaline phosphatase (AP), glutamate dehydrogenase (GLDH) and the concentrations of bilirubin in blood plasma after a single intraruminal application of aflatoxins were studied in four dairy cows. The maximum changes in the activities of the enzymes and the maximum bilirubin concentration in plasma were obtained in the first two to three days following the application of aflatoxins. The statistically significant increase of GOT activity, compared with activity before the application of aflatoxins, persisted until the 23rd day; in the case of LDH and GLDH the increase persisted until the 38th day from the application of aflatoxins. The activities of gamma-GTP and AP were slightly higher even on the 50th day. The increased concentration of bilirubin in plasma lasted until the 23rd day from aflatoxin application. The increased activities of enzymes testify to an impaired function of the liver, which is also proved by the specific enzymes GLDH, gamma-GTP, by increased bilirubin levels, and by histological changes known from literature. The evaluation of enzymatic activities and bilirubin concentration in plasma can make a valuable contribution to correct diagnosis of aflatoxicoses in cattle.
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PMID:[Changes in enzyme activity induced by experimental aflatoxicosis in dairy cows]. 1 36

Seventeen serum markers (including 9 enzyme activities) for eventual tissue damage were studied after ESWL in 40 patients with unilateral kidney calculosis. No changes were established in the 8 non-enzymic parameters and the activities of amylase, lipase, AST (GOT), ALT (GPT) and CK-MB. A statistically significant increase was found in LDH, alpha-HBDH, CK (twice) and glutamate dehydrogenase (3 times). The slight elevation of LDH and alpha-HBDH could be due to haemolysis caused by the shock waves. Increased activity of CK suggested myolysis and that of GlDH a hepatocellular damage.
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PMID:Acute changes of serum markers for tissue damage after ESWL of kidney stones. 188 66

The toxic potential of sodium orthovanadate towards isolated perfused rat livers was investigated at a dose of 2 mmol/l. In livers from fasted rats, vanadate led to a release of cytosolic (glutamate-pyruvate-transaminase (GPT) and lactate dehydrogenase (LDH] and mitochondrial (glutamate dehydrogenase (GLDH] enzymes, an accumulation of calcium in the liver, a marked depletion of hepatic glutathione and an enhanced release of it into the perfusate, as well as an augmented formation and release of thiobarbituric acid-reactive material by the liver. Furthermore, a marked inhibition of oxygen consumption was observed. Vanadate-induced vasoconstriction resulted in a progressive decrease in perfusate flow rate. Control experiments with similarly reduced flow rates led to a comparable reduction in oxygen consumption. GPT and LDH release and hepatic glutathione depletion were also evident, though to a lesser extent than in the presence of vanadate, but no increase in GLDH release, in tissue calcium content or TBA-reactive material in the liver or the perfusate were observed. Thus, indirect toxic effects due to a reduced flow rate contribute only partly to vanadate hepatotoxicity and do not affect mitochondrial integrity. Omission of calcium from the perfusate did not prevent hepatotoxic responses to vanadate, although less calcium was present in the treated livers than in the control organs, indicating that calcium influx is not involved in vanadate-induced hepatotoxicity in the intact organ, in contrast to isolated hepatocytes. Feeding the animals, resulting in an activation of anaerobic energy conservation reactions, strongly attenuated vanadate hepatotoxicity indicating that the energetic status of the liver is the main target of vanadate. Superoxide dismutase did not affect the hepatotoxic responses of livers from fasted rats towards vanadate, while allopurinol and deferrioxamine inhibited lipid peroxidation and hepatotoxicity due to vanadate. The strong correlation between induction of lipid peroxidation and hepatotoxicity and the inhibition of both processes in parallel by antioxidants are suggestive of a causative role for lipid peroxidation in vanadate-induced hepatotoxicity.
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PMID:Vanadate-induced toxicity towards isolated perfused rat livers: the role of lipid peroxidation. 199 68

The behavior of cytoplasmic and mitochondrial enzymes has been studied in rat liver at 1, 5, and 24 hr after 60 min of ischemia using histochemical methods. This period of ischemia resulted 24 h after ischemia in liver cell necrosis in about 15% of the volume of the ischemic liver lobes. As early as after 1 hr reperfusion lactate dehydrogenase (LDH, cytoplasm) activity decreased in a certain proportion of the liver parenchymal cells, whereas glutamate dehydrogenase (GDH, mitochondrial matrix) activity started to decrease after 5 hr reperfusion; the activities of mitochondrial membrane enzymes, monoamine oxidase and succinate dehydrogenase, did not decrease before 24 hr of reperfusion. It has been concluded that the early decrease in LDH activity is caused by leakage into the blood and reflects reversible damage; when this decrease is accompanied by a decrease in GDH activity irreversible liver cell damage is assumed. Diminished activity of mitochondrial membrane enzymes, due to leakage and denaturation, is observed when real necrosis can be assessed.
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PMID:Changes in cytoplasmic and mitochondrial enzymes in rat liver after ischemia followed by reperfusion. 367 63

Lactate (LDH) and succinate (SDH) dehydrogenases activities decreased in red and white muscles of rat under acute ethanol loading indicating the inhibition of energy metabolism and stepped up lactic acid formation under stress conditions. Aspartate aminotransferase (AAT) and glutamate dehydrogenase (GDH) were found to increase. In contrast to these, the AMP deaminase activity decreased in white muscle suggestive of decreased deamination of nucleic acids. The ornithine cycle enzymes such as argininosuccinate synthetase (ArSS) and arginase indicated diminished activities showing low level of operation of urea cycle and consequent accumulation of ammonia was observed in red muscle with low production of glutamine, whereas in the case of white muscle this trend is reversed. The possible alterations of ethanol toxicity on energy requirements, transdeamination patterns, ureogenesis and glutamine production have been discussed.
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PMID:Metabolic alterations in the red and white muscles of rat to acute ethanol treatment. 618 32

Sciatectomized toad gastrocnemius has shown a progressive loss in lactate (LDH), succinate (SDH) and malate (MDH) dehydrogenase activities and elevation of glutamate dehydrogenase (GDH) activity during post-neurectemic days. The possible role of malate in the restoration of metabolic homeostasis in denervated muscle is discussed.
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PMID:Alterations in some dehydrogenase profiles of sciatectomized toad gastrocnemius muscle-metabolic modifications by malate. 651 66

Previous studies have capitalized on ordered kinetic mechanisms in the design of biospecific affinity chromatographic methods for highly efficient purifications and mechanistic studies of enzymes. The most direct tactic has been the use of immobilised analogues of the following, usually enzyme-specific substrates, e.g., lactate/pyruvate in the case of lactate dehydrogenase for which NAD+ is the leading substrate. Such immobilised specific substrates are, however, often difficult or impossible to synthesise. The locking-on strategy reverses the tactic by using the more accessible immobilised leading substrate, immobilised NAD+, as adsorbent with soluble analogues of the enzyme-specific ligands (e.g., lactate in the case of lactate dehydrogenase) providing a substantial reinforcement of biospecific adsorption sufficient to effect adsorptive selection of an enzyme from a group of enzymes such as the NAD(+)-specific enzymes. The value of this approach is demonstrated using model studies with lactate dehydrogenase (LDH, EC 1.1.1.27), alcohol dehydrogenase (ADH, EC 1.1.1.1), glutamate dehydrogenase (GDH, EC 1.4.1.3) and malate dehydrogenase (MDH, EC 1.1.1.37). Purification of bovine liver GDH in high yield from crude extracts is described using the tactic.
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PMID:Further studies on the bioaffinity chromatography of NAD(+)-dependent dehydrogenases using the locking-on effect. 891 27

The activities of Na+,K(+)-ATPase in plasma membrane, of cytosolic enzymes and of glutamate dehydrogenase (GlGD) in mitochondria were measured in leukocytes (WBC) from dogs and cats to clarify the differences in energy metabolism in these cells. Feline WBC had significantly higher activities of hexokinase (HK), pyruvate kinase (PK) and LDH with pyruvate as substrate than did canine WBC. Canine WBC had significantly higher activities of glucokinase (GK) and GlDH than did feline WBC. Feline WBC had unique characteristics of energy metabolism in that the activities of the cytosolic enzymes under anaerobic conditions were significantly higher than those in canine WBC. It therefore appears that there are distinct differences in glucose-metabolism in WBC between dogs and cats. WBC enzyme activities are considered to reflect the metabolic state in the whole body of the animal. It is therefore suggested that changes in the activities of certain glycolytic enzymes in WBC may be useful as a diagnostic indicator in some types of metabolic disease in dogs and cats.
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PMID:A comparison of the activities of certain enzymes related to energy metabolism in leukocytes in dogs and cats. 961 90

The kinetic locking-on strategy utilizes soluble analogues of the target enzymes' specific substrate to promote selective adsorption of individual NAD(+)-dependent dehydrogenases on their complementary immobilized cofactor derivative. Application of this strategy to the purification of NAD(+)-dependent dehydrogenases from crude extracts has proven that it can yield bioaffinity systems capable of producing one-chromatographic-step purifications with yields approaching 100%. However, in some cases the purified enzyme preparation was found to be contaminated with other proteins weakly bound to the immobilized cofactor derivative through binary complex formation and/or nonspecific interactions, which continuously "dribbled" off the matrix during the chromatographic procedure. The fact that this problem can be overcome by including a short pulse of 5'-AMP (stripping ligand) in the irrigant a couple of column volumes prior to the discontinuation of the specific substrate analogue (locking-on ligand) is clear from the results presented in this report. The general effectiveness of this auxiliary tactic has been assessed using model studies and through incorporation into an actual purification from a crude cellular extract. The results confirm the usefulness of the stripping-ligand tactic for the resolution and purification of NAD(+)-dependent dehydrogenases when using the locking-on strategy. These studies have been carried out using bovine liver glutamate dehydrogenase (GDH, EC 1.4.1.3), yeast alcohol dehydrogenase (YADH, EC 1.1.1.1), porcine heart mitochondrial malate dehydrogenase (mMDH, EC 1.1.1.37), and bovine heart L-lactate dehydrogenase (l-LDH, EC 1.1.1.27).
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PMID:A "stripping" ligand tactic for use with the kinetic locking-on strategy: its use in the resolution and bioaffinity chromatographic purification of NAD(+)-dependent dehydrogenases. 1042 64

A new method for the determination of branched-chain alpha-ketoacid concentration using lactate dehydrogenase (E C 1.1.1.27) isozyme C4 (LDH C4) from mouse testes is proposed. The assay is performed on urine and plasma without previous treatment. Alpha-ketoglutarate and pyruvate are determined on the same sample using glutamate dehydrogenase (GDH, EC 1.4.1.2) and lactate dehydrogenase isozyme A4 (LDH5) respectively and subtracted from the total alpha-ketoacid concentration obtained with LDH C4. This value corresponds to the branched chain alpha-ketoacid. Results were linear within the concentration range 8 to 170 mumoles/L. Detection limit was 8 mumoles/L. Analytical recovery was higher than 91%. For microplate assays, recoveries were higher than 84% and the detection limit was 20 mumoles/L. Determinations performed with GDH, LDH A4 and LDH C4 allow differentiation of E3 deficiency from other clinical phenotypes of maple syrup urine disease. The method is simple and fast, and adaptation to microplates would allow screening of newborns.
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PMID:Enzymatic method for branched chain alpha-ketoacid determination: application to rapid analysis of urine and plasma samples from maple syrup urine disease patients. 1079 48


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