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 damaging effects of ADP/Fe/NADPH-induced lipid peroxidation were studied on the enzymes and membranes of rat liver mitochondria. Succinate, an inhibitor of mitochondrial lipid peroxidation, prevented or delayed most of the damage caused by the peroxidation on different mitochondrial structures and functions. There were marked abnormalities on the electrophoretic pattern of mitochondrial proteins during the course of lipid peroxidation. The disappearance of particular polypeptide bands and the accumulation of high-molecular-weight aggregates could be observed. Succinate was found to delay these effects. As a consequence of lipid peroxidation the succinate oxidase activity of mitochondria was decreased. The succinate dehydrogenase enzyme and the component(s) of the respiratory chain were inactivated. Succinate prevented the inactivation of succinate dehydrogenase but did not protect the other components of terminal oxidation chain. From the matrix enzymes the glutamate dehydrogenase retained its full activity but the NADP-linked isocitrate dehydrogenase was inactivated. The mitochondrial membranes became permeable to large protein molecules. Succinate prevented the inactivation of isocitrate dehydrogenase and delayed the release of protein molecules from mitochondria.
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PMID:Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation. 303 29

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

The metabolic pathways of glucose were studied by histochemical reactions in some species of gastropods living in different habitats. The glycolytic pathway is histochemically indicated by positive results for glucose-6-phosphate isomerase, fructose-1,6-biphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, and D-lactate dehydrogenase. The enzymes of the Krebs cycle gave different responses: isocitrate dehydrogenase and L-malate dehydrogenase were positive, whilst succinate dehydrogenase was constantly negative. Malate synthetase activity was also demonstrated. Despite L-glutamate dehydrogenase is undetectable, the presence of transaminase indicates the gluconeogenetic route. Phosphoglucomutase and glucose-6-phosphate phosphatase appear also positive. The metabolic meaning of our results were discussed.
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PMID:Histochemical research on metabolic pathways of glucose in some species of Mollusca Gastropoda. 311 Nov 50

Molecular mass, Stoke's radius, frictional coefficient and isomer-type of non-denatured proteins can be obtained by time-dependent gradient gel electrophoresis by evaluating the resulting data using a two-step mathematical procedure. Provided a histochemical staining procedure is available to locate the position of an enzyme in the gel, crude cell extracts can be used for estimating their molecular size properties. The computation of molecular properties of non-denatured proteins is demonstrated for isozymes of aspartate aminotransferase (EC 2.6.1.1), peroxidase (EC 1.11.1.42) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) from current-year needles of spruce. The resulting data as well as those which were calculated for esterase (EC 3.1.1.1), glutamate dehydrogenase (EC 1.4.1.4), isocitrate dehydrogenase (EC 1.4.1.42), and shikimate dehydrogenase (EC 1.1.1.25) are in accordance with those reported in the literature. The method described may be applied to various scientific areas such as genetics or environmental pollution. It could be shown here that current-year needles of injured spruce (damage class 3) contained two more peroxidase isozymes and one more glucose-6-phosphate dehydrogenase isozyme than those from non-injured trees. These differences may mark two genotypes of spruce of different susceptibilities towards present-day air and soil pollutants.
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PMID:Determination of molecular mass, Stokes' radius, frictional coefficient and isomer-type of non-denatured proteins by time-dependent pore gradient gel electrophoresis. 323 69

The interactive effects of lima bean trypsin inhibitor (TI), hemagglutinin (Hgg) and cyanide (CN) when fed at the same degree of activity as found in the raw lima bean (RLB) were assessed in weanling rats using hepatic glutamate dehydrogenase (GLDH), isocitrate dehydrogenase (ICDH), ornithine carbamoyltransferase (OCT) and intestinal disaccharidases activities as the response criteria. Whereas RLB significantly (P less than 0.05) increased hepatic GLDH and decreased ICDH activities respectively, dietary CN, TI and Hgg whether acting individually or jointly had no significant influence on GLDH. Only the CN-containing diets significantly (P less than 0.05) elevated ICDH activity when compared with the control. Raw lima bean significantly (P less than 0.05) depressed OCT activity while neither the individual nor collective effects of these factors were significant. Dietary CN + TI + Hgg interaction depressed maltase activity to approximately the same extent as RLB in all the intestinal regions. These factors had neither individual nor collective effects on sucrase in the small intestine. Lactase activity in the small intestine was influenced only by the RLB diet, while CN + Hgg, and CN + TI + Hgg dietary combinations induced significant (P less than 0.05) elevations in the activities of cellobiase when compared with the control. Although synergism of action is indicated in a number of instances, it is suggested that these factors may need to combine with others within the bean, perhaps synergistically, to elicit comparable anti-nutritional influences as the RLB.
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PMID:The interactive effects of lima bean (Phaseolus lunatus) trypsin inhibitor, hemagglutinin and cyanide on some hepatic dehydrogenases, ornithine carbamoyltransferase and intestinal disaccharidases in weanling rats. 324 17

Normal human platelets have been separated according to density on continuous Percoll gradients and the platelet distribution divided into five fractions containing approximately equal numbers of platelets. The mean volumes and protein contents of the platelets in each fraction were found to correlate positively with density while the protein concentration did not differ significantly between the fractions. Four mitochondrial enzymes (monoamine oxidase, glutamate dehydrogenase, cytochrome oxidase and NADP-dependent isocitrate dehydrogenase) were assayed and their activities per unit volume were found to increase in a very similar monotonic fashion with platelet density. When MAO and GDH were assayed on the same set of density fractions the correlation between the two activities was very high (r = 0.94-1.00, p less than 0.001) and a similar close correlation was found between MAO and ICDH. The results support the hypothesis that high density platelets either have a higher concentration of mitochondria or have larger mitochondria than low density platelets.
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PMID:Monoamine oxidase and other mitochondrial enzymes in density subpopulations of human platelets. 336 31

The assay of cerebrospinal fluid (CSF) enzymes has been suggested for assessing the extent of damage and patient prognosis in cases of brain injury. A potential difficulty associated with using CSF enzyme levels as predictors of outcome is the possibility that enzyme concentrations may vary substantially from one brain region to another. We have determined the concentrations of seven enzymes in seven brain regions in the rat and cat. Acid phosphatase (ACP), aspartate aminotransferase (AST), isocitrate dehydrogenase (ICDH), lactate dehydrogenase (LD), and malate dehydrogenase (MDH) show little regional variability in the rat and cat while creatine kinase (CK) and glutamate dehydrogenase (GDH) both exhibit considerable regional variability in both animals. Lack of correlation between CSF enzyme levels and prognosis may possibly be explained by the observed regional variability. The enzymes demonstrating more homogeneous concentrations throughout the brain may be better candidates for predicting patient outcome by determination of the CSF enzyme level.
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PMID:The regional variability of enzymes in the brain: relevance to CSF enzyme determinations. 341 84

Direct transfer of NADPH between two NADP-dependent dehydrogenases, isocitrate dehydrogenase and glutamate dehydrogenase, has been investigated. These enzymes have opposite stereospecificity for hydrogen transfer to the coenzyme. In contrast with the general direct-transfer mechanism postulated for NAD-dependent dehydrogenases [Srivastava & Bernhard (1986) Science 234, 1081-1086], no evidence for direct transfer in either direction was found for these NADP-dependent dehydrogenases.
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PMID:Absence of direct coenzyme transfer in an A-B dehydrogenase system. 343 43

Glutamate dehydrogenase (GDH, EC 1.4.1.2) has long been used as a marker for mitochondria in brain and other tissues, despite reports indicating that GDH is also present in nuclei of liver and dorsal root ganglia. To examine whether GDH can be used as a marker to differentiate between mitochondria and nuclei in the brain, we have measured GDH by enzymatic activity and on immunoblots in rat brain mitochondria and nuclei which were highly enriched by density-gradient centrifugation methods. The activity of GDH was enriched in the nuclear fraction as well as in the mitochondrial fraction, while the activities of other "mitochondrial" enzymes (fumarase, NAD-isocitrate dehydrogenase and pyruvate dehydrogenase complex) were enriched only in the mitochondrial fraction. Immunoblots using polyclonal antibodies against bovine liver GDH confirmed the presence of GDH in the rat brain nuclear and mitochondrial fractions. The GDH in these two subcellular fractions had a very similar molecular weight of 56,000 daltons. The mitochondrial and nuclear GDH differed, however, in their susceptibility to solubilization by detergents and salts. The mitochondrial GDH could be solubilized by extraction with low concentrations of detergents (0.1% Triton X-100 and 0.1% Lubrol PX), while the nuclear GDH could be solubilized only by elevated concentrations of detergents (0.3% each) plus KCl (greater than 150 mM). Our results indicate that GDH is present in both nuclei and mitochondria in rat brain. The notion that GDH may serve as a marker for mitochondria needs to be re-evaluated.
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PMID:The subcellular localization of glutamate dehydrogenase (GDH): is GDH a marker for mitochondria in brain? 352 73

We used high-resolution polyacrylamide gradient gel electrophoresis (PGGE) to separate four babesial enzymes to aid in the identification of two Babesia microti isolates established in hamsters. The isolates were compared to two different hamsters passages of the "Gray" strain. All isoenzymes patterns from the two isolates and the "Gray" strain were similar except glucose phosphate isomerase (GPI) from one of the "Gray" strain passages. It showed a polymorphic GPI pattern as opposed to a monomorphic GPI pattern seen in the other "Gray" strain passage and the two isolates. The observed differences suggested that some population of B. microti are capable of having polymorphic GPI, that the "Gray" strain originally contained (and may still contain) a heterogeneous population of B. microti, and that the population possessing polymorphic GPI was selected over that with monomorphic GPI. This information was obtained by a PGGE method that eliminated hemoglobin from gels and allowed, for the first time, detection of babesial leucine amino peptidase (LAP) and isocitrate dehydrogenase (IDH). In addition, this method provided molecular weight estimations on babesial GPI, LAP, IDH, and glutamate dehydrogenase (GDH), and it proved useful in the identification and characterization of the B. microti isolates.
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PMID:Isoenzyme analysis of Babesia microti infections in humans. 373 51


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