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 time of expression of the paternal genes of glutamate dehydrogenase (GDH), lactate dehydrogenase (LDH) and acetylcholine esterase (AChE) was investigated in the development of fish hybrids. The species which differed by the thermostability of homologous enzymes were selected as parental pairs. The appearance of differences in the thermostability of homologous enzymes between the hybrids and the maternal species suggested the beginning of paternal enzyme synthesis in the hybrid embryos. Differences in the AChE thermostability appeared simultaneously with the enzyme activity at the stage of first muscle contractions (35 hrs of development), differences in the mitochondrial GDH thermostability appeared at the stage of hatching (50-60 hrs) and those in the LDH thermostability 12-17 days after hatching. The total activity of AChE and GDH sharply increased during the period of the paternal enzyme appearance whereas the activity of LDH suffered practically no changes. Differences in the AChE thermostability between the hybrids and the maternal species are the same for both the total AChE (in supernatant, 15,000 gX10 min.) and the solubilised AChE (in supernatant, 130,000 gX60 min.). AChE of the parental species and the hybrids have the same electrophoretic mobility. The differences in the thermostability of enzymes are preserved following the electrophoresis in polyacrilamide gel.
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PMID:[Expression of the paternal genes for lactate dehydrogenase, glutamate dehydrogenase and acetylcholinesterase in the development of hybrid fish between species from the families of Cobitidae and Cyprinidae]. 102 8

Because of the difficulties in drawing blood for clinical chemistry in small laboratory animals there exist many methods for sampling blood and the preparation of serum, none of which is generally accepted or well standardised. It was the aim of this study to investigate the effects of sampling techniques on normal values of enzyme activities in the serum of rat and mouse. The activities of the following enzymes were determined: sorbitol dehydrogenase, lactate dehydrogenase, malate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, pyruvate kinase, creatine kinase, myokinase, alkaline phosphatase and leucine aminopeptidase. In addition plasmaproteins, urea and inorganic phosphorus were measured. In rats blood was obtained from the following sites: retroorbital venous plexus, jugular vein, heart and ventral aorta. In mice blood was sampled from the jugular vein and the ventral aorta. Shifts of water from the interstitial to the intravascular space due to hypovolemia occurring during the experimental procedure were followed up by measuring the hematocrit and the distribution of radioiodide labelled albumin. In rats the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase, pyruvate kinase, creatine kinase and myokinase found in blood serum obtained from the retroorbital venous plexus and the ventral aorta were too high compared to the other sampling sites. Activities of alkaline phosphatase and alanine aminotransferase were slightly elevated when blood was sampled from the punctured retroorbital venous plexus. Small differences in plasmaproteins and hematocrit values were found to be due to acute shifts of water within the extracellular space. In mice the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and myokinase were found to be too high in blood serum obtained from the ventral aorta. Efflux of enzymes from damaged cells and the interstitial space ive caused erroneous results too, but only to a minor extent. The most reliable method for blood sampling in rat and mouse is the cannulation of the jugular vein. The heart puncture can be recommended too. Attention should be paid, however, to the possibility of aspirating disrupted muscle cells through the inserted needle.
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PMID:[Effects of blood sampling on enzyme activities in the serum of small laboratory animals (author's transl)]. 108 84

Two groups of rats were given aspirin and phenacetin in their food at daily doses similar to those taken by humans suffering from analgesic abuse. Both drugs damaged the kidney proximal tubules although phenacetin affected the kidney more severely than aspirin. At the start of the experiment aspirin increased the urinary excretion of lactate dehydrogenase (LDH) while phenacetin raised the excretion of all four enzymes studies (acid phosphatase, alkaline phosphatase, glutamate dehydrogenase (GDH), LDH indicating generalised cellular injury. Subsequent samples of urine collected from rats up to seven weeks showed normal urinary enzyme levels. The value of urinary enzyme measurements in detecting renal damage by drugs is discussed.
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PMID:Urinary enzymes and kidney damage by aspirin and phenacetin. 112 62

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49

The effects of the organic osmolyte beta-dimethylsulfoniopropionate (DMSP) on the structural stability of three model proteins were examined to determine whether DMSP, like the structurally similar solute dimethyl sulfoxide (DMSO), is compatible with native protein structure at low, but not elevated, temperatures. DMSP stabilized phosphofructokinase under conditions of cold-induced denaturation. Thus, DMSP, like DMSO, may be an effective protein cryoprotectant. However, DMSP was not an effective stabilizer of protein structure under conditions of heat denaturation. Whereas low (0.2 M) concentrations of DMSP stabilized lactate dehydrogenase against inactivation at 50 degrees C, higher DMSP concentrations were ineffective. DMSP favored the denaturation of glutamate dehydrogenase at all DMSP concentrations tested. DMSP may be a compatible osmotic solute only under conditions of moderate temperature and low, yet physiological, concentrations. The mechanistic basis of DMSP's temperature- and concentration-dependent effects and the possible roles played by adaptation temperature and severity of osmotic stress in the evolutionary selection of organic osmolytes are discussed.
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PMID:Temperature- and concentration-dependence of compatibility of the organic osmolyte beta-dimethylsulfoniopropionate. 129 91

The determination of ammonia in plasma, using glutamate dehydrogenase, is complicated by non-specific oxidation of the coenzyme, promoted by components of the sample matrix. Measurements performed with appropriate plasma blanks show that 2'-phosphorylated coenzymes (NADPH, deamino-NADPH) are much less oxidized than NADH. By adding lactate dehydrogenase, NADH oxidation by endogenous pyruvate can be completed within a short time. Considerable consumption of coenzyme occurs, however, and endogenous L-alanine aminotransferase also represents a possible source of interference. The results of ammonia determinations using deamino-NADPH (y) or NADPH (x) were identical (a = 0.0 mumol/l, b = 1.00; r = 0.996, n = 62). With NADH as the coenzyme, the method displays adequate specificity only at high sample dilution, e.g. in the measurement of urea after conversion to ammonia.
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PMID:Which is the appropriate coenzyme for the measurement of ammonia with glutamate dehydrogenase? 145 16

The activities of six enzymes associated with carbohydrate metabolism were measured both in carcinomas and in normal breast tissues. The following differences were observed. 1. The carcinoma showed higher enzyme activities than the normal mammary tissue. 2. The ratios of glutamate dehydrogenase, hydroxybutyrate dehydrogenase, glutathione reductase and catalase to lactate dehydrogenase were lower in carcinomas than in normal tissues. Similarly, the ratios of glutamate dehydrogenase, hydroxybutyrate dehydrogenase, glutathione reductase and catalase to glucose-6-phosphate dehydrogenase were also significantly lower in carcinomas. 3. There were no significant differences in enzyme activities between I and II stage of the disease and the metastatic tissues, however, there were significant differences between I and III stage. The significance of these findings is discussed in terms of the alterations in the balance between the metabolic pathways.
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PMID:Enzyme activities in human breast tumours. 148 90

The ubiquinone systems and electrophoretic comparison of enzymes were used to determine the relatedness among 64 isolates of seven Aspergillus spp. These were 31 clinical and 3 nonclinical isolates of Aspergillus fumigatus Fres., 2 isolates of A. nidulellus Samson & W. Gams, 8 isolates of A. terreus Thom, 4 isolates of A. flavus Link, 1 isolate of A. oryzae (Ahlburg) Cohn, 14 isolates of A. niger van Tieghem, and 1 isolate of A. japonicus Saito. The enzymes glucose 6-phosphate dehydrogenase, lactate dehydrogenase, glutamate dehydrogenase, fumarase, and malate dehydrogenase were examined. The relative mobilities were analyzed numerically. The results were presented as a dendrogram. Isolates from clinical and nonclinical sources within the same species had identical ubiquinone systems and identical or very similar enzyme patterns. In the dendrogram, 64 of the tested isolates were separated into seven major clusters at a 60% similarity level. Each major cluster corresponds to a single species. On the dendrogram, A. fumigatus isolates showed homogeneity, whereas A. niger isolates showed relative heterogeneity; in particular, A. niger MF-24 and the other A. niger isolates were distantly linked to each other. All A. fumigatus isolates had the Q-10 ubiquinone system and formed a single major cluster at a similarity level of 73% or greater. Glucose 6-phosphate dehydrogenase and glutamate dehydrogenase were key enzymes for differentiating all clinical and nonclinical isolates of A. fumigatus from the other Aspergillus spp. Ubiquinone systems and enzyme patterns appear to be objective and useful indicators for use in the precise identification of clinical isolates of Aspergillus spp.
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PMID:Application of ubiquinone systems and electrophoretic comparison of enzymes to identification of clinical isolates of Aspergillus fumigatus and several other species of Aspergillus. 150 May 6

Incubation of isolated rat hepatocytes with 0.1 mM iron nitrilotriacetic acid (FeNTA) caused a rapid rise in lipid peroxidation followed by a substantial increase in trypan blue staining and lactate dehydrogenase release, but did not affect the protein and non-protein thiol content of the cells. Hepatocyte death was preceded by the decline of mitochondrial membrane potential, as assayed by rhodamine 123 uptake, and by the depletion of cellular ATP. Chelation of extracellular Ca2+ by ethylene glycol bis(beta-aminoethyl ether) N,N'-tetraacetic acid or inhibition of Ca2+ cycling within the mitochondria by LaCl3 or cyclosporin A did not prevent the decline of rhodamine 123 uptake. On the other hand, a dramatic increase in the conjugated diene content was observed in mitochondria isolated from FeNTA-treated hepatocytes. Oxidative damage of mitochondria was accompanied by the leakage of matrix enzymes glutamic oxalacetic aminotransferase (GOT) and glutamate dehydrogenase (GLDH). The addition of the antioxidant N,N'-diphenylphenylene diamine (DPPD) completely prevented GOT and GLDH leakage, inhibition of rhodamine 123 uptake, and ATP depletion induced by FeNTA, indicating that Ca(2+)-independent alterations of mitochondrial membrane permeability consequent to lipid peroxidation were responsible for the loss of mitochondrial membrane potential. DPPD addition also protected against hepatocyte death. Similarly hepatocytes prepared from fed rats were found to be more resistant than those obtained from starved rats toward ATP depletion and cell death caused by FeNTA, in spite of undergoing a comparable mitochondrial injury. A similar protection was also observed following fructose supplementation of hepatocytes isolated from starved rats, indicating that the decline of ATP was critical for the development of FeNTA toxicity. From these results it was concluded that FeNTA-induced peroxidation of mitochondrial membranes impaired the electrochemical potential of these organelles and led to ATP depletion which was critical for the development of irreversible cell injury.
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PMID:Mitochondrial damage and its role in causing hepatocyte injury during stimulation of lipid peroxidation by iron nitriloacetate. 163 73

Previously, the synthesis and validation of [32P]2N3NAD+ as an active site directed photoaffinity probe for glutamate dehydrogenase (GDH) was reported (8). This report shows that 2N3NAD+ is also an effective probe for the NAD+ binding site of lactate dehydrogenase (LDH). With the appropriate photolabeling procedures and immobilized boronate column chromatography the active site peptides of GDH and LDH involved in the adenine base binding domain have been isolated and sequenced. With both GDH and LDH a single photolabeled peptide, which contained the majority of the photoinserted radiolabel, was isolated. Additionally, these peptides had UV spectra that were markedly different from the nonphotolabeled peptides. The modified peptide from GDH corresponded to Cys270 through Lys289. Both sequencing and compositional analysis identified Glu275 as the site of photoinsertion. Sequencing of this peptide aborted at Glu275 after five rounds of analysis, indicating that insertion was blocking further progress. Compositional analysis showed that the entire sequence from residues 270 to 289 was present except that the single Glu residue was missing. This is interpreted as indicating that the photoinsertion is into the polypeptide backbone at the Glu site. The peptide isolated from LDH corresponded to Asp82 through Arg90. Sequencing of this peptide could be completed throughout with only the round at Tyr83 giving no identifiable residue. Compositional analysis of this peptide was in agreement with the peptide from Asp82 to Arg90 with the exception that the single Tyr residue was missing. This indicates that the photoinsertion is into the tyrosine side chain. This data was found to be in agreement with X-ray crystallographic results identifying the NAD(+)-binding domains.
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PMID:Identification of peptides in the adenine ring binding domain of glutamate and lactate dehydrogenase using 2-azido-NAD+. 168 10


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