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)

Sensitive, precise, and rapid methods for the measurement of alcohol dehydrogenase (ADH) and glutamate dehydrogenase (GDH) were developed on the Cobas Bio centrifugal analyser. The optimal pH for ADH in caucasians was 9.8. Non-linearity of ADH enzyme activity was observed when samples were diluted in saline; linearity was restored when inactivated serum was used as diluent. ADH was shown to be a sensitive index of liver anoxia due to cardiorespiratory disturbance (clinical sensitivity 90%) and generalised anoxia. GDH exhibited sensitivity equal to that of alanine aminotransferase (ALT) but was inferior to gamma-glutamyltransferase (GGT) in the detection of specific liver disease. Both ADH and GDH were sensitive indicators of alcoholic liver disease.
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PMID:Adaptation of methods for glutamate dehydrogenase and alcohol dehydrogenase activities to a centrifugal analyser: assessment of their clinical use in anoxic states of the liver. 289 Jun 62

Intact rat liver cells from the perivenous region were isolated by collagenase perfusion after first destroying the periportal region by a brief portal infusion of digitonin. Periportal cells were isolated after retrograde digitonin infusion. Significantly higher alanine aminotransferase, gamma-glutamyltransferase and lactate dehydrogenase activities and lower glutamate dehydrogenase and pyruvate kinase activities in periportal than in perivenous cells demonstrate marked separation. The high yield allows further characterization in vitro of the cell populations.
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PMID:Digitonin-collagenase perfusion for efficient separation of periportal or perivenous hepatocytes. 299 54

To study the severity and degree of in utero alcohol effects in relation to the rate of maternal alcohol damage, multiparous 1-year alcohol-fed rats were used, with an appropriate pair-fed control group. During pregnancy, alcoholic dams showed relatively high acetaldehyde levels (41 +/- 19 mumol/l) and blood alcohol levels of 22.8 +/- 14 mmol/l. They also showed marked histological alterations in liver as well as high serum aspartate-aminotransferase, alanine-aminotransferase, alkaline phosphatase, glutamate dehydrogenase, and gamma-glutamyltransferase activities. The increase in serum enzyme levels did not correlate with an increase in hepatic enzyme levels since only glutamate dehydrogenase was enhanced in liver after 1 year of alcohol intake. In addition, except for an increase in low Km aldehyde dehydrogenase activity, there were no changes in liver alcohol metabolizing enzymes in chronic alcohol vs. pair-fed females. Alcoholic rats showed a high incidence of damage in their progeny (resorptions, immature fetuses, decrease in fetal weight, etc.), and rats with the highest serum levels of the above enzymes (especially glutamate dehydrogenase and gamma-glutamyl transferase) had severely affected progeny. Rats with minimal histological liver damage, in contrast, did not show resorptions. Thus, the results presented suggest that the stage of maternal alcohol illness, as indicated mainly by the extent of liver damage, plays an important role in the frequency and severity of in utero alcohol effects in the rat.
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PMID:The role of maternal alcohol damage on ethanol teratogenicity in the rat. 342 5

Using fully mechanized analytical equipment, interference by haemolysis in the determination of 26 clinical chemical parameters was determined quantitatively by adding haemolysate to serum. Haemoglobin concentrations up to 6.6 g/l caused essentially no interference in the following determinations: albumin (immuno-nephelometric), alpha-amylase, calcium, chloride, cholesterol, cholinesterase, creatinine, iron, glucose, glutamate dehydrogenase, uric acid, urea, sodium, inorganic phosphate, total protein, transferrin and triglycerides. In the presence of haemoglobin, erroneously high values were found for: lactate dehydrogenase (haemoglobin higher than 0.2 g/l), aspartate aminotransferase, potassium and acid phosphate (haemoglobin higher than 1.5 g/l), creatine kinase (haemoglobin higher than 2.5 g/l) and alanine aminotransferase (haemoglobin higher than 3.4 g/l). Erroneously low values were found for bilirubin (haemoglobin higher than 0.8 g/l), alkaline phosphatase and albumin (by electrophoresis) (haemoglobin higher than 1.5 g/l) and gamma-glutamyltransferase (haemoglobin higher than 3.0 g/l).
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PMID:Haemolysis as an interference factor in clinical chemistry. 371 97

Previous observations that valproic acid (VPA) causes hepatic damage prompted us to investigate the effect of large doses of the drug (0.6, 1.2 and 1.8 mmol/kg/day) on a number of liver enzymes located on different subcellular fractions. In mitochondria, glutamate dehydrogenase, aspartate aminotransferase and ornithine carbamoyltransferase were significantly increased (1.8 mmol/kg/day). In microsomes, gamma-glutamyltransferase activity increased significantly (1.8 mmol/kg) and cytochrome P-450 content decreased significantly (1.2 and 1.8 mmol/kg). In cytosol, both aspartate and alanine aminotransferase activities were increased at all dose levels. These results indicate that VPA induces dose-dependent changes in some liver enzyme activities.
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PMID:Effect of sodium valproate on subcellular fraction enzymes in rat liver. 393 26

We measured the activities of two mitochondrial enzymes, the mitochondrial form of aspartate aminotransferase (EC 2.6.1.1) and glutamate dehydrogenase (EC 1.4.1.2), in the serum of apparently healthy persons (n = 84) and patients suffering from chronic liver diseases (n = 43). The distribution of activities for glutamate dehydrogenase, but not mitochondrial aspartate aminotransferase, was sex-dependent. The upper limits of the reference intervals (99th percentile) at 37 degrees C were 3.2 U/L for mitochondrial aspartate aminotransferase, 6.4 U/L for glutamate dehydrogenase (women), and 11.0 U/L for glutamate dehydrogenase (men); there was a weak correlation between the activities of both mitochondrial enzymes (r = 0.439). In patients with chronic liver diseases we found a greater increase in the activity of glutamate dehydrogenase than of mitochondrial aspartate aminotransferase and the correlation between the two mitochondrial enzymes was stronger. The diagnostic sensitivity and specificity of either mitochondrial enzyme was less than that of total aspartate aminotransferase, alanine aminotransferase (EC 2.6.1.2), or gamma-glutamyltransferase (EC 2.3.2.2).
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PMID:Mitochondrial enzymes in human serum: comparative determinations of glutamate dehydrogenase and mitochondrial aspartate aminotransferase in healthy persons and patients with chronic liver diseases. 396 54

1. Aspergillus nidulans, Neurospora crassa and Escherichia coli were grown on media containing a range of concentrations of nitrate, or ammonia, or urea, or l-glutamate, or l-glutamine as the sole source of nitrogen and the glutamate dehydrogenate and glutamine synthetase of the cells measured. 2. Aspergillus, Neurospora and Escherichia coli cells, grown on l-glutamate or on high concentrations of ammonia or on high concentrations of urea, possessed low glutamate dehydrogenase activity compared with cells grown on other nitrogen sources. 3. Aspergillus, Neurospora and Escherichia coli cells grown on l-glutamate possessed high glutamine synthetase activity compared with cells grown on other nitrogen sources. 4. The hypothesis is proposed that in Aspergillus, Neurospora and Escherichia colil-glutamate represses the synthesis of glutamate dehydrogenase and l-glutamine represses the synthesis of glutamine synthetase. 5. A comparison of the glutamine-synthesizing activity and the gamma-glutamyltransferase activity of glutamine synthetase in Aspergillus and Neurospora gave no indication that these fungi produce different forms of glutamine synthetase when grown on ammonia or l-glutamate as nitrogen sources.
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PMID:Regulation of synthesis of glutamate dehydrogenase and glutamine synthetase in micro-organisms. 490 26

The activities of lactate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, beta-galactosidase, N-acetyl-beta-D-glucosaminidase, leucine aminopeptidase, gamma-glutamyltransferase and alkaline phosphatase in renal tissue and urine of rats treated with sodium tetrathionate were determined. A decrease of enzyme activities in renal tissue and an increase in urine were observed. The largest decrease in the glutamate dehydrogenase of renal tissue amounted to 0.7 times the control value, and was correlated with an appropriate increase in the urine. Increases in urinary enzyme activity were especially marked for beta-galactosidase and N-acetyl-beta-D-glucosaminidase (3 and 6 times the control values, respectively). The increase in enzyme activities was not accompanied by a corresponding change in the urinary protein. Characterization of urinary lactate dehydrogenase and N-acetyl-beta-D-glucosaminidase isoenzymes also indicates the renal origin of these enzymes. The abnormally high enzyme activities of the urine correlated with the nature and degree of renal damage shown by electron microscopy.
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PMID:Effect of sodium tetrathionate on the activities of some enzymes in kidney and urine. 611 89

Compared with controls, patients with alcoholic fatty liver showed a significant increase of gamma-glutamyltransferase activity both in the liver and serum, whereas alkaline phosphatase activity was raised only in the liver but not in the serum. The activities of other enzymes such as aspartate aminotransferase, alanine aminotransferase and glutamate dehydrogenase remained virtually unchanged in the liver of patients with alcoholic fatty liver but were strikingly enhanced in the serum. The hepatic and serum alterations of enzymic activities observed in patients with alcoholic fatty liver could be reproduced in the rat model of alcoholic fatty liver only for gamma-glutamyltransferase but not for the other enzymes tested, substantiating evidence that the animal model may serve as an appropriate tool for studying interactions between alcohol and gamma-glutamyltransferase. The present experiments also indicate that the primary cause for increased serum gamma-glutamyltransferase activities associated with prolonged alcohol consumption is hepatic enzyme induction rather than liver cell injury.
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PMID:Hepatic gamma-glutamyltransferase activity in alcoholic fatty liver: comparison with other liver enzymes in man and rats. 613 56

Alcoholism is a common disease; it is found in 10% to 15% of all patients admitted to general hospitals. There is no single characteristic finding, but on the other hand, changes as compared with normal values have been reported in the literature for more than 30 frequently assayed clinical chemical and haematological parameters. In the project reported here all 24 clinical chemical parameters and all 8 haematological parameters frequently assayed were studied in each of 82 hospitalized men with a confirmed diagnosis of alcoholism. The diagnosis of alcoholism was made on the basis of the Munich Alcoholism Test (MALT) together with the following standardized assessments and examinations: past history, an alcohol questionnaire, general physical examination and neurological examination. All forms were filled in completely. All steps in the clinical laboratory investigations were standardized, and all were subject to ongoing reliability control. The clinical problem is usually not to differentiate alcohol abusers or alcoholics from healthy persons but rather to identify the alcoholics among a population of patients with a variety of illnesses. For this reason 70 patients from two hospitals who were clearly neither alcohol abusers nor alcoholics were studied in exactly the same manner as the alcoholics. In this combined group of 152 hospitalized patients significant differences were found in the distribution of the values for the alcoholics and the non-alcoholics for the following clinical chemical and haematological parameters: at the 0.1% level gamma-glutamyltransferase, aspartate aminotransferase, urea, creatinine and mean corpuscular volume (MCV), and at the 1% level glutamate dehydrogenase, alanine aminotransferase and alkaline phosphatase. From these eight parameters those combinations of between two and six parameters were selected that discriminated best between the alcoholics and the non-alcoholics. Using conventional decision limits the following was found: For the alcoholics two or more of the results for the following five parameters were outside the decision limits given in parentheses: gamma-glutamyltransferase (greater than or equal to 28 U/l), aspartate aminotransferase (greater than or equal to 18 U/l), alanine aminotransferase (greater than or equal to 22 U/l), MCV (greater than or equal to 96 fl), creatinine (less than or equal to 66.3 mumol/l). The diagnostic sensitivity (alcoholics) is 85%, the diagnostic specificity (non-alcoholics) is 64%.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Detection and exclusion of alcoholism in men on the basis of clinical laboratory findings. 614 78


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