Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.49 (glucose-6-phosphate dehydrogenase)
 7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hepatocytes were prepared from 15 degrees C acclimated catfish (Ictalurus punctatus) and maintained in primary culture for 20 days on biomatrix at 7, 15, and 25 degrees C without hormones or serum to determine if cells can directly adapt to temperature. Specific activities of cytochrome-c oxidase, NADH-cytochrome c reductase, citrate synthase, and glucose-6-phosphate dehydrogenase showed acclimatory rate compensation (7 greater than 15 greater than 25 degrees C cultured); 6-phosphogluconate dehydrogenase had activity changes of 15 greater than 7 greater than 25 degrees C cultured; activity of lactate dehydrogenase occurred in the series 7 greater than 15 = 25 degrees C. Protein synthesis of freshly isolated hepatocytes from catfish acclimated to the three temperatures exhibited acclimatory rate compensation. In contrast, protein synthesis of cultured hepatocytes occurred in the series 15 greater than 25 greater than 7 degrees C cultured. Protein degradation was highest at 25 degrees C followed by cells at 15 and 7 degrees C. Cultured hepatocytes showed incomplete temperature acclimation in vitro by way of enzyme activity changes and of protein synthesis. This suggests that some factor(s), such as hormones, is probably necessary to mediate the full temperature-acclimation process.
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PMID:Can cultured teleost hepatocytes show temperature acclimation? 300 35

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 levels of ATP, ADP, AMP, NADP, NADPH, NAD, NADH and reduced glutathione were determined in the red blood cells of individuals with glucose-6-phosphate dehydrogenase (G6PD) deficiency, beta-thalassemia (beta-thal) heterozygotes and in a boy carrying both mutations. The results obtained confirmed a reduced concentration of NADPH in G6PD deficiency and showed that with the combination of both diseases, the red blood cell contained practically undetectable levels of NADPH. Assays of some red blood cell enzyme activities known to be markedly influenced by cell age suggested that a younger mean red cell population is present in beta-thal/G6PD deficiency. Thus, the marked oxidative stress caused by beta-thal, that is apparently incompatible with G6PD deficiency, in fact exists, probably because of the residual activity of this enzyme in the younger red cells.
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PMID:Redox and energetic state of red blood cells in G6PD deficiency, heterozygous beta-thalassemia and the combination of both. 309 52

The new calcium antagonist anipamil (1,7-bis-(3-methoxyphenyl)-3-methylaza-7-cyano-nonadecane) exhibited a pronounced protective effect against isoprenaline-induced myocardial necrosis in rats. Anipamil was administered in single doses of 10 or 20 mg/kg daily for 4 days. 30 mg/kg isoprenaline was given by subcutaneous injection on the 3rd and 4th days of the study. The protective effect of anipamil was assessed by histological investigations, and its effect on the activity of the enzymes succinate dehydrogenase, NADH-NBT reductase, acid phosphatase and glucose-6-phosphate dehydrogenase in experimentally-induced myocardial damage was assessed quantitatively by microphotometry. The protective effect of anipamil against isoprenaline-induced myocardial necrosis was definitely dose-dependent: 10 mg/kg anipamil exhibited a partial protective effect, whilst 20 mg/kg anipamil protected the heart completely.
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PMID:Protective effect of the new calcium antagonist anipamil against isoprenaline-induced cardionecrosis in rats. 313 Aug 38

Possible protective effects of Allium sativum and Crataegus--alone and in combination--on isoprenaline (isoproterenol)-induced heart, liver and pancreas damage were studied using rats as test animals. Pretreatment with Allium sativum alone, or in combination with Crataegus, resulted in protective effects on isoprenaline-induced damage of heart, liver, and pancreas. These effects proved to be dose-dependent. The following parameters were used to evaluate the protective effect: Clinical signs, qualitative histological and histoenzymatical findings, as well as quantitative microphotometric determination of enzymatic activities of succinate dehydrogenase, NADH-NBT reductase, acid phosphatase and glucose-6-phosphate dehydrogenase in cardiac, hepatic and pancreatic tissues. The underlying mechanisms are discussed. The results suggest that Allium sativum, resp. Allium sativum plus Crataegus exert a pronounced protective effect.
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PMID:The protective effect of Allium sativum and crataegus on isoprenaline-induced tissue necroses in rats. 321 41

Fundamental aspects of the reduction of tetrazolium salts were investigated and, in particular, the role of oxygen in the reduction. It was found that oxygen had a competitive inhibitory effect on the reduction of (Tetra)Nitro BT mediated by NADH and phenazine methosulphate. This competitive effect, under aerobic conditions, could be reversed by using tetrazolium concentrations of 5 mM. Oxygen did not have a significant effect on BPST reduction, whereas the inhibitory effect of oxygen on the reduction of Neotetrazolium was not reversed by increasing the tetrazolium concentration. The oxygen effect on Nitro BT reduction was considerably less when macromolecular substances such as albumin or polyvinyl alcohol were added to the medium. This may be due to increased Nitro BT concentrations being built up at the surface of macromolecules due to the nonpolar components of the Nitro BT molecule. When demonstrating glucose-6-phosphate dehydrogenase activity in vitro or in tissue sections with the use of Nitro BT, oxygen also had a direct inhibitory effect, even when azide was added to the medium for the inhibition of flavoprotein-mediated electron transfer to oxygen. Again, this direct inhibition of Nitro BT reduction by oxygen could be excluded by using a high Nitro BT concentration. Macromolecules present in the incubation medium or in tissue sections counteracted the oxygen effect. It is concluded that the maximum reaction rate and optimum localization of dehydrogenases is obtained when histochemical media are used containing 5 mM (Tetra)Nitro BT and 20% polyvinyl alcohol.
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PMID:On the role of oxygen in dehydrogenase reactions using tetrazolium salts. 322 Jul 95

Co-immobilization methods have been developed for a bienzymatic system of luminescent Beneckea harveyi bacteria with formate dehydrogenase, glucose-6-phosphate dehydrogenase, and phosphoglucomutase. Bioluminescent assays have been devised for NADH, NAD, FMN, glucose 6-phosphate, and glucose 1-phosphate using the co-immobilized enzyme preparation. The lowest detection limits were in the picomole range with the bacterial extract and in the femtomole range with the partially purified enzymes, bacterial luciferase, and NADH:FMN oxidoreductase.
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PMID:Bioluminescent microassay of various metabolites using bacterial luciferase co-immobilized with multienzyme systems. 326 18

We studied energy metabolism after experimental subarachnoid hemorrhage in rats. Four different cerebral areas were tested: frontal cortex, occipital cortex, hippocampus, and brainstem. Vmax of the following enzymatic activities was evaluated: in the homogenate: hexokinase, phosphofructokinase, and lactate dehydrogenase for the glycolytic pathway, and glucose-6-phosphate dehydrogenase for the hexose monophosphate shunt; in the purified nonsynaptic mitochondria: NAD+-isocitrate dehydrogenase, citrate synthase, and succinate dehydrogenase for the Krebs cycle, and cytochrome oxidase for the electron transfer chain. We also evaluated some parameters related to the respiration of nonsynaptic mitochondria (State 3, State 4, uncoupled state, respiratory control ratio, and ADP:O ratio). Subarachnoid hemorrhage did not significantly affect Vmax of the enzymatic activities related to anaerobic and aerobic metabolism; however, mitochondrial respiration was affected, particularly in the presence of NADH-producing substrates (glutamate + malate).
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PMID:Bioenergetics of different brain areas after experimental subarachnoid hemorrhage in rats. 335 25

Muscle biopsies from six horses with clinical histories of muscle atrophy, muscle tremors, myopathic symptoms, unsteadiness of pelvic limbs and progressive ataxia were examined. Muscle biopsies were studied with enzyme histochemical techniques to evaluate the diagnostic values of these methods in cases suspected of suffering from neuromuscular disorders. Hypertrophy, atrophy, fibre splitting, waxy degeneration, phagocytosis and necrosis were seen in haematoxylin eosin stained sections of the different cases. Fibre type predominance and fibre type grouping were seen in the calcium ion stimulated myosine ATP-ase (Ca-ATP-ase) stained sections of some cases. 'Moth-eaten fibres' were demonstrated in three cases by staining with NADH: nitro blue tetrazolium oxidoreductase (NADH-TR), succinate dehydrogenase (SDH), NADH dependent malate dehydrogenase, cytochrome c oxidase and by lactate dehydrogenase. The catabolic enzymes, acid phosphatase (ACP) and 5'-nucleotidase were active in cases with fibre phagocytosis. The oxidative part of the pentose phosphate pathway in myopathic tissue seemed to be important in three cases, demonstrated by the increased activity of glucose-6-phosphate dehydrogenase (GPDH) and 6-phosphogluconate dehydrogenase (PGDH). The important feature of diseased horse muscle was that the pathohistochemical changes were exactly the same as in diseased skeletal muscles of humans. The application of tissue saving enzyme histochemical techniques can be recommended in the study of muscle tissue from horses suffering from suspected neuromuscular disorders.
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PMID:Enzyme histochemistry on muscle biopsies as an aid in the diagnosis of diseases of the equine neuromuscular system: a study of six cases. 336 6

We describe a bioluminescent immunoassay procedure which does not require a separation step to remove excess free label. A luminescent immunosorbent constituted of bacterial luciferase, FMN oxidoreductase, and an antibody coimmobilized on Sepharose is used to determine specifically the label enzyme (glucose-6-phosphate dehydrogenase, coupled to an antigen) bound by a specific antibody. The immunosorbent confines the bioluminescent reaction in a small volume, and the bound label produces NADH, which is directly used by the nearby luciferase FMN oxidoreductase enzyme system. On the contrary NADH produced by dehydrogenases in solution is directly oxidized without emitting light. Dehydrogenases contained in the biological sample do not interfere with the assay, which can be performed directly on 25 microliter of serum. In this paper we describe the general procedure and we analyze the different parameters that must be optimized.
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PMID:Bioluminescent immunosorbent for rapid immunoassays. 351 35


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