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:1.6.99.3 (diaphorase)
5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rabbits given 1 ppm of vanadate in drinking water for twelve months showed (a) increased plasma levels of catecholamines (b) reduction of the arterial concentration of nitric oxide (c) lower activity of urine kallikrein and higher activities of urine kininases I and II and enkephalinase (d) reduced cardiac inotropism and augmented total peripheral resistance, with unchanged blood pressure levels (e) accumulation of the metal in the aorta and cardiac ventricles. Monoaminooxidase and glucose-6-phosphate dehydrogenase activities were increased by vanadate in both kidney and liver and that of NADH-diaphorase in the kidney, in which NADPH-diaphorase activity was reduced. Some of the above results were also obtained in rats given 10 and 40 ppm of vanadate in drinking water for six-seven months; these animals showed arterial hypertension and reduced activity of Na, K-ATPase in the kidney. Vanadium appears to act on the cardiovascular function through selective neurohumoral, autacoidal and transductional mechanisms only in part depending on the species.
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PMID:[Neurohumoral, autacoid and transductional mechanisms in the cardiovascular effects of vanadate: histochemical correlations]. 937 36

The localisation of diaphorase was visualised by light microscopy using the dye nitro blue tetrazolium and NADPH as substrates. Under appropriate conditions, diaphorase reduces this dye to a dark blue insoluble formazan. The enzyme was located at very low activity in many tissue and glandular structures of the deer, but at very much higher activity in sebaceous glands in the dermal velvet of the antler and skin, and in additional sebaceous gland-related structures in the ear canal, prepuce and tail (scent) gland. Within sebaceous glands, activity was greatest in the outermost layers of the acini, but decreased as the cells progressed and differentiated centripetally. There was little or no difference between the staining observed when NADH was used as a substrate, compared to NADPH. There was generalised staining (usually light) for glucose-6-phosphate dehydrogenase, lactate dehydrogenase, and glycerol-3-phosphate dehydrogenase. However, this staining was not specifically localised to sebaceous glands and related structures, showing that the observed activity in these structures was due to a diaphorase that was distinct from any of the dehydrogenase activities tested. The possible role of diaphorase in sebaceous development and secretion is discussed.
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PMID:Diaphorase activity in sebaceous glands and related structures of the male red deer. 1042 9

Sensitivity to various oxidants was determined for Escherichia coli strains JTG10 and 821 deficient in biosynthesis of glutathione (gsh-) and their common parental strain AB1157 (gsh+). The three strains showed identical sensitivity to H2O2. E. coli 821 was more resistant than AB1157 and JTG10 to menadione, cumene hydroperoxide, and N-ethylmaleimide. This resistance was not related to the gsh mutation because the other gsh- mutant and the parental strain showed similar sensitivity to these oxidants. The measured activities of NADPH:menadione diaphorase and glucose-6-phosphate dehydrogenase and the extracellular level of menadione suggested that the enhanced resistance of E. coli 821 to menadione might be due to decreased diaphorase activity, but not to a lowered rate of menadione uptake.
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PMID:Oxidative stress resistance of Escherichia coli strains deficient in glutathione biosynthesis. 1056 56

Twelve enzymes from mature pollen grains of maize were separated by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The separation in the second dimension was both in the presence and absence of sodium dodecyl sulfate (SDS). Ten of the investigated enzymes lost activity after separation in the presence of SDS, but those of esterases and acid phosphatase could be recovered. On the other hand, 2-D electrophoresis without SDS is suitable for the analysis of maize pollen pectinesterase, malate dehydrogenase, glutamic-oxalacetic transaminase, diaphorase, superoxide dismutase, and phosphoglucose isomerase. 1-D PAGE and isoelectric focusing (IEF) are sufficient to analyze glucose-6-phosphate dehydrogenase, alcohol dehydrogenase, shikimic dehydrogenase, and glutamate dehydrogenase. The possibility of applying 2-D electrophoresis for the analysis of enzymes from single stigma and stigma exudate is dicussed.
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PMID:Maize pollen enzymes after two-dimensional polyacrylamide gel electrophoresis in the presence or absence of sodium dodecyl sulfate. 1182 13

This paper describes the development of a novel optically interrogated enzyme electrode with generic applicability for NAD(P) dependent enzymes. The example reported here employs a multi-enzyme pathway comprising the enzymes pyruvate kinase, hexokinase, glucose-6-phosphate dehydrogenase and diaphorase. The final substrate of this pathway, dichlorophenol indophenol (DCPIP), was immobilised within an ultra-thin polymer film of o-phenylenediamine, itself electrochemically polymerised onto a conductive gold coating on the surface of a support polyethylene sheet. Dichlorophenol indophenol (DCPIP) absorbs within the visible region of the spectrum with a lambda(max) approximately 600 nm. When reduced, the molar absorption coefficient at this wavelength decreases significantly and DCPIP effectively becomes colourless (DCPIPH(3)). Ultra-thin layers of gold (<10 nm thickness) exhibit an optical absorption minimum at wavelengths of approximately 520 nm and therefore light within this region of the spectrum may be transmitted with relative ease through the polymer/gold/polyethylene optrode. Results presented within this paper show how this electro-optical sensor may be used to determine concentrations of adenosine triphosphate (ATP) within a sample. In the presence of ATP a colour change from blue to colourless was observed for DCPIP when the assay was performed in solution. However, when DCPIP was immobilised within a polymeric film onto the surface of gold coated electrodes, a colour change from blue to red was observed corresponding to a third redox state of DCPIP (DCPIPH).
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PMID:A novel electro-optical sensor format with generic applicability for exploitation with NAD(P) dependent enzymes. 1270 65

Simmons, R. J. (Michigan State University, East Lansing), and R. N. Costilow. Enzymes of glucose and pyruvate catabolism in cells, spores, and germinated spores of Clostridium botulinum. J. Bacteriol. 84:1274-1281. 1962.-An investigation was made of the enzymes of vegetative cells, spores, and germinated spores of Clostridium botulinum 62-A to elucidate a pathway of glucose metabolism. Manometric studies were conducted with intact cells, and various enzymes and enzyme systems were assayed in cell-free and spore-free extracts by use of spectrophotometric and colorimetric procedures. Glucose fermentation was found to be inducible; glucokinase was the controlling enzyme. All other enzymes of the Embden-Meyerhof-Parnas (EMP) pathway were found in both induced and non-induced cells, but they were in relatively low concentrations in the latter. This, plus the fact that no glucose-6-phosphate dehydrogenase was detected, led to the conclusion that glucose is catabolized primarily by the EMP system. A number of glycolytic enzymes were also found in extracts of spores and germinated spores of this organism, but the activities were extremely low as compared with activities in cell extracts. A phosphoroclastic-type reaction was readily demonstrated in both glucose-adapted and non-adapted cells, but not in spores and germinated spores. However, both acetokinase and phosphotransacetylase, as well as coenzyme A transphorase, were detected in spores and germinated-spore extracts, although at very low activity levels as compared with cell extracts. The specific activity of diaphorase in spore extracts was about one-half that of corresponding cell extracts, and the activity of reduced diphosphopyridine nucleotide (DPNH) oxidase was actually higher in the spore extracts. In addition, the DPNH oxidase in spore extracts was considerably more heat-stable than that in extracts of cells or germinated spores.
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PMID:Enzymes of glucose and pyruvate catabolism in cells, spores, and germinated spores of Clostridium botulinum. 1397 33

A nonradioisotope, 96-well-microplate assay to evaluate glucose uptake activity in cultured cells has been developed. 2-Deoxyglucose (2DG) was detected by measuring a potent fluorophore, resorufin, generated after incubation with a single assay solution containing hexokinase, adenosine 5'-triphosphate, glucose 6-phosphate dehydrogenase, beta-nicotineamide adenine dinucleotide phosphate, diaphorase, and resazurin. This amplifying detection system could detect the fluorescence intensity induced by uptake of 2DG into L6 skeletal muscle cells, even at the level of cells cultivated in individual wells in a 96-well microplate. Using this assay system, the effects of insulin, cytochalasin B (hexose uptake inhibitor), LY294002 (inhibitor of glucose transporter translocation), and pioglitazone hydrochloride (insulin-sensitizing agent) on 2DG uptake into L6 myotubes could be assessed clearly. Therefore, our simple method may be useful for in vitro high-throughput screening and for evaluating regulators of glucose uptake.
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PMID:A nonradioisotope, enzymatic assay for 2-deoxyglucose uptake in L6 skeletal muscle cells cultured in a 96-well microplate. 1644 89

Naringenin is a flavanone that is believed to have many biological actions, including as an anti-oxidant, free radical scavenger and an antiproliferative agent. The global incidence of gastric carcinoma is increasing rapidly, more than for any other cancer. Therefore, in the present study, we tested the effects of naringenin on gastric carcinogenesis induced by N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) and saturated sodium chloride (S-NaCl) in rats. Male Wistar rats were divided into five groups and treated over a period of 20 weeks as follows: (i) a control group given corn oil (1 mL/rat, p.o.) daily 20 weeks; (ii) 200 mg/kg, p.o., MNNG on Days 0 and 14 with S-NaCl (1 mL/rat) administered twice a week for the first 3 weeks; (iii) 200 mg/kg, p.o., MNNG on Days 0 and 14, with naringenin (200 mg/kg, p.o., daily) treatment for the entire 20 weeks; (iv) 200 mg/kg, p.o., MNNG on Days 0 and 14, with naringenin treatment (200 mg/kg, p.o., daily) initiated from 6 to 20 weeks; (v) 200 mg/kg, p.o., naringenin alone daily for 20 weeks. In Group II rats in which gastric cancer was inducted with MNNG and S-NaCl, there was a significant increase in hydrogen peroxide and lipid peroxidation levels, with decreases in reduced glutathione, oxidized glutathione, glutathione peroxidase, glutathione reductase and glucose 6-phosphate dehydrogenase. In addition, in Group II rats with gastric cancer, there were significant increases in the activity of cytochrome P450, cytochrome b(5) and NADPH cytochrome c reductase, with concomitant decreases in the activity of the phase II enzymes glutathione S-transferase and UDP-glucuronosyl transferase. Naringenin treatment (Groups III and IV) restored enzyme activity to near control levels. These results indicate that naringenin has a chemopreventive action against MNNG-induced gastric carcinoma in experimental rats.
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PMID:Modulatory effect of naringenin on N-methyl-N'-nitro-N-nitrosoguanidine- and saturated sodium chloride-induced gastric carcinogenesis in male Wistar rats. 1856 95

Two enzyme reactors prepared by the co-immobilization of two different glucose-6-phosphate dehydrogenases (G6PDH; from Leuconstoc mescenteroides (LM) and yeast (Y) and diaphorase are employed to enhance the sensitivity of NAD(P) coenzymes as on-line amplifiers based on substrate recycling in a chemiluminometric flow-injection system. The NAD(P) coenzymes are recycled enzymatically during passage through the reactor in the presence of sufficient glucose-6-phosphate and oxygen in the carrier solution to produce a large amount of hydrogen peroxide, which is detected chemiluminometrically in the subsequent flow line. The G6PDH(LM)/diaphorase co-immobilized reactor is not specific between the NAD and NADP coenzymes, but shows a six fold selectivity towards NADP coenzymes compared to NAD coenzymes; the amplification factors for NAD and NADP coenzymes are 60 and 380, respectively, at a flow rate of 0.3 ml min(-1). In contrast, the G6PDH(Y)/diaphorase co-immobilized reactor is specific for NADP coenzymes with an amplification factor of about 600 (at a flow rate of 0.3 ml min(-1)). The detection limit is 6 fmol for both NADP(+) and NADPH.
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PMID:Highly selective and sensitive detection of NADP coenzymes using co-immobilized glucose-6-phosphate dehydrogenase/diaphorase reactors as on-line amplifiers based on substrate recycling in a chemiluminometric flow-injection system. 1896 58

The aim of the present work was to evaluate structural and metabolic changes in histaminergic neurons in hypothalamic nucleus E2 in rats in conditions of complete external drainage of bile. Studies were performed on male Wistar rats (n = 45). Controls consisted of animals subjected to sham surgery with preservation of physiological bile flow throughout the experiment. Quantitative histological and histochemical methods were used. Serial frontal cryostat sections cut from the posterior hypothalamus were used for detection of the activity of the following enzymes: monoamine oxidase B, succinate dehydrogenase, NADH dehydrogenase, NADPH dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase, and acid phosphatase. Morphological studies of histaminergic neurons were performed on preparations stained with thionine. These studies showed that complete external drainage of bile led to transient size reductions and rounding of cell perikarya. Metabolic changes were seen within a day of bile loss and subsequently progressed. All energy metabolic pathways were suppressed and acid phosphatase activity was increased on day 5.
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PMID:Structural-metabolic changes in histaminergic neurons of the rat hypothalamus in conditions of loss of bile. 1897 11


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