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)

Histochemical studies of some myocardial oxido--reductive enzymes after a beta--adrenergic blockade with propranolol have been carried out. Succinate, isocitrate and glucose-6-phosphate dehydrogenases did not indicate any changes in activity, whereas the changes in reaction intensities concerning NADH and NADPH tetrazole reductases and glutamate dehydrogenase have rather a transitory and reversible character. Only lactate dehydrogenase showed an increase in the enzymatic activity which speaks for an increase in the glycolysis process in the heart muscle. In the light of our own presented research results we assume that the experimental beta--adrenergic blockade of the heart muscle in rats does not evoke more important enzymatic changes which are noticeable in histochemical microscope examination.
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PMID:Histochemical studies of some myocardial oxido-reductive enzymes after experimental beta-adrenergic blockade with propranolol. 21 81

The changes induced by phenobarbital in cerebral enzymatic activities of the Krebs' cycle (citrate synthase, malate dehydrogenase) and electron transfer chain (total NADH-cytochrome c reductase and cytochrome oxidase) were studied. In addition, the activity of lactate dehydrogenase of acetylcholine esterase and of glutamate dehydrogenase was also studied. These enzymatic activities were evaluated in the homogenate in toto and in a crude mitochondrial fraction from rat brain. The modifications in some of these activities indicate that several new metabolic situations occur in brain tissue after phenobarbital treatment.
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PMID:Effect of phenobarbital on cerebral energy state and metabolism. Enzymatic activities. 23 Jun 18

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
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PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

The effect of boseimycin on the in vitro activity and in vivo synthesis of alkaline phosphatase, aconitase and lactate, isocitrate, glutamate and alanine dehydrogenases was studied in Bacillus subtilis. At a subinhibitory concentration, synthesis of glutamate dehydrogenase was stimulated but alkaline phosphatase, lactate dehydrogenase and aconitase synthesis was inhibited. On the contrary, boseimycin inhibited slightly the activity of lactate dehydrogenase in cell-free extracts. Glutamate dehydrogenase and aconitase activities were not affected.
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PMID:Effect of boseimycin on some enzyme systems of Bacillus subtilis. 24 Jul 61

Use of the gel film technique in microphotometric determinations of enzyme activity is described. The microscope photometer is computer-controlled. It is programmed to deal with repetitive measurements at up to 12 selected positions within a tissue section and to evaluate recorded reaction rates statistically. Films of polyacrylamide gel with entrapped glucose-6-phosphate dehydrogenase are used as a model to demonstrate the correlation between local enzyme activity and the microphotometrically determined reaction rate. Enzyme activities at different positions in the same tissue section are determined and compared. Activity profiles of five enzymes (glutamate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, NAD-dependent tetrazolium reductase) in the liver are presented and show non-uniform intra-acinar distribution patterns. These results are interpreted in the light of the metabolic zonation of the hepatic acinus. Further applications of the method are discussed.
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PMID:Microphotometric determination of enzyme activities in cryostat sections by the gel film technique. 26 70

Electrophoretic variation of the enzymes glucose phosphate isomerase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase and glutamate dehydrogenase (NADP-dependent) has been studied in the African murine malaria parasites Plasmodium berghei, P. yoelii, P. vinckei and P. chabaudi and their subspecies. Horizontal starch gel electrophoresis was used throughout. The number of isolates examined in each subspecies varied from 1 (P. y. nigeriensis) to 24 (P. c. chabaudi). Extensive enzyme variation was found among isolates of most of the subspecies from which more than two such isolates were available for study. It is clear that the phenomenon of enzyme polymorphism is of common occurrence among malaria parasites. With the exception of P. berghei and P. yoelii, of which all isolates share an identical electrophoretic form of lactate dehydrogenase, no enzyme forms are shared between any of the 4 species of murine plasmodia. By contrast, within each species common enzyme forms are shared among each of the subspecies. The subspecies are nevertheless, distinguished from each other by the electrophoretic forms of at least one enzyme. The distribution and reassortment of enzyme variation among isolates of a single subspecies is in accordance with the concept of malaria parasites as sexually reproducing organisms. The study of variation among parasites present in individual wild-caught rodent hosts demonstrates that natural malarial infections usually comprise genetically heterogeneous populations of parasites. Nevertheless, the number of genetically distinct types of parasite of any one species present in a single infected host appears to be small. Generally not more than 2 or 3 clones of parasite of distinct genetic constitution are present in a single infected animal.
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PMID:Studies on enzyme variation in the murine malaria parasites Plasmodium berghei, P. yoelii, P. vinckei and P. chabaudi by starch gel electrophoresis. 35 25

For the evaluation of certain differences in the diminution of export proteins of the liver we examined some exactly defined groups of liver diseases with the aim of further differentiation of the pathogenetic mechanisms. We measured the activity of glutamate-oxalacetate transaminase, glutamate-pyruvate transaminase, glutamate dehydrogenase, lactate dehydrogenase, alkaline phosphatase, cholinesterase and lecithin-cholesterol acyltransferase, the Quick value, the coagulation factors I, II, V, VII, VIII, IX and X. Clotting factors were determined by a Schnitger-Gross Coagulometer. Prothrombin, antithrombin III, plasminogen, factor VIII associated antigen and activated factor XIII were measured by immunoelectrophoresis according to Laurell. Lipoprotein electrophoresis in agarose gel was performed to evaluate changes in lecithin-cholesterol acyltransferase activity. Except of the rising diminution of export proteins in the course of liver disease from acute hepatitis to cirrhosis we found also specific changes of the patterns of the plasma specific enzymes. These proteins were diminished dependent on their half life time and the inflammatory activity--measured as the height of the transaminases. Lecithin cholesterol acyltransferase and factor VIII did not participate in the general diminution of the most export proteins; some details were found to explain this differing behaviour. Results are critically discussed with regard to new aspects in the biochemistry of the damaged liver cell.
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PMID:[Correlations between the diminished secretion of export proteins from the liver and the plasmatic activity of liver cell enzymes (author's transl)]. 42 91

The hepatocyte and haematopoietic cell contents of the liver of the foetal guinea pig were measured over the latter half of gestation. Hepatocytes represented about 30% of liver volume at mid-gestation and this increased to 70-80% by term; cell volume remained fairly constant until 5-7 days before term, then more than doubled. Haematopoietic cells represented about 5% of liver volume at mid-gestation and this progressively fell to <1% by term. At 75% of gestation hepatocytes and haematopoietic cells were prepared from perfused foetal livers by collagenase digestion. Enzyme activity of the hepatocyte was, without exception, similar to that of the whole liver. In general, enzyme activity in the haematopoietic cells was similar to that in erythrocytes, with relatively low values for aldolase, glycerol 3-phosphate dehydrogenase, phosphoglycerate mutase, enolase, lactate dehydrogenase, phosphoenolpyruvate carboxykinase, fructose 1,6-bisphosphatase, isocitrate dehydrogenase, ;malic' enzyme, glutamate dehydrogenase and aspartate aminotransferase. The haematopoietic cell contribution to total enzyme activity in the foetal liver was usually much less than 10% and could thus not account for the major changes in hepatic enzyme activity over the latter half of gestation. Hepatocytes contained hexokinase isoenzymes I and III, aldolase isoenzymes A and B and pyruvate kinase isoenzymes 1, 2 and 4. The haematopoietic cells contained hexokinase isoenzyme I and two additional bands of activity with slightly greater mobility, aldolase isoenzyme A and pyruvate kinase isoenzymes 2 and 4.
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PMID:The distribution of enzyme and isoenzyme activities between parenchymal and haematopoietic cells in the liver of the foetal guinea pig. 43 88

The relative sensitivity of urinary enzyme measurements for detecting renal damage was determined for two nephrotoxins. Injection of a single dose of sodium phosphate (10 mmoles/kg) caused damage to the proximal tubules and led to a 15 fold increase in lactate dehydrogenase (LDH) activity excreted into the urine. In contrast to this change the serum LDH remained normal. Similar results were obtained following the injection of cephaloridine (2 g/kg) with an 18 fold increase in urinary LDH and a marginal increase in urinary glutamate dehydrogenase (GDH). By contrast the serum LDH was unchanged. Urinary enzymes are therefore more sensitive for detecting renal injury than enzymes. The four enzymes investigated are located in specific regions of the cell so that the involvement of the organelles and regions of the cell can be followed. Damage to the organelles does not appear to occur as the excretion of the lysosomal enzymes remained normal and only in the case of cephaloridine were marginal changes in the mitochondrial GDH excretion seen. The average alkaline phosphatase was also normal suggesting no gross damage to the plasma membrane although a few individual rats excreted abnormal activities of alkaline phosphatase. These rats however, also excreted high activities of LDH. This suggests that damage to the membrane causes leakage of LDH and in severe cases release of the plasma membrane enzyme alkaline phosphatase. The administration of cephaloridine at various doses showed that urinary enzyme measurements were as sensitive as histology for demonstrating renal damage and that of these enzymes, LDH was by far the most useful.
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PMID:The sensitivity of urinary enzyme measurements for detecting renal injury. 44 87

Intraacinar distribution of succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NADP-dependent isocitrate dehydrogenase (IDH), glutamate dehydrogenase (GluDH), lactate dehydrogenase (LDH) and NADH-tetrazolium dehydrogenase (TR) was studied in rat liver cryostat sections by multipositional microphotometric activity determinations. By statistical evaluation, activity of individual enzymes could be related to the acinar topography. Activity was evaluated with regard to distance of measuring position either from afferent (portal) or efferent (hepatic) vessels. Two independent distribution curves were obtained for each enzyme. Acinar distribution of all the enzymes studied followed sigmoid courses with maximal activity of SDH, MDH and LDH in zone 1 ("periportal") and GluDH, IDH, TR in zone 3 ("pericentral"). For all enzymes, maximum activity gradients were confined to zone 2 of the acinus. Data were also evaluated as ratios of activities in zone 1 and zone 3. The following ratios zone 1/zone 3 were obtained: SDH = 1.9, MDH = 1.7, IDH = 0.5, GluDH = 0.5, LDH = 1.3 and TR = 0.6.
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PMID:Microphotometric studies on intraacinar enzyme distribution in rat liver. 52 13


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