Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

In cerebellum of the adult rat, glucose-6-phosphate dehydrogenase (G6PD) activity is particularly localized in Purkinje cells, showing lower activity in the molecular and granule cell layers. G6PD is the first and rate-limiting step of the hexose monophosphate shunt (HMS), which has the physiological role of providing NADPH for reductive biosynthesis and detoxifying reactions. In this study, we searched for a possible correlation between G6PD and other NADPH-consuming enzymes, such as NADPH-cytochrome P450 reductase (P450R), glutathione reductase (GR) and NADPH-diaphorase (NADPH-d). This study was performed by means of immunohistochemistry and enzyme histochemistry followed by quantitative densitometric and confocal laser scanning microscopic analyses. Our results demonstrated that G6PD, P450R and GR have a similar distribution pattern characterized by the highest concentration of these enzymes in the somata of Purkinje cells, and by lower concentrations in the molecular and the granule cell layers. Moreover, in Purkinje cells, G6PD colocalized with both P450R and GR. NADPH-d activity showed a different distribution pattern when compared to the other enzymes, revealing the highest activity in the molecular layer and the lowest in Purkinje cells. Our results suggest a coordinated regulative mechanism of G6PD, P450R and GR based on the request of NADPH or on specific transcription factors.
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PMID:NADPH-consuming enzymes correlate with glucose-6-phosphate dehydrogenase in Purkinje cells: an immunohistochemical and enzyme histochemical study of the rat cerebellar cortex. 1568 Oct 36

The resistance to oxidative stress is a multifactorial reaction involving the clustering of transcriptionally regulated genes. Because glucose-6-phosphate dehydrogenase (G6PD), the principal enzyme responsible for reducing power, is highly expressed in the olfactory bulb (OB), it is of interest to verify whether other enzymes utilizing NADPH are also highly expressed. The level and localization of G6PD- and NADPH-consuming enzymes, such as NADPH-cytochrome P450 oxidoreductase (P450R), glutathione reductase (GR), and NADPH-diaphorase (NADPH-d), were analyzed in the rat olfactory bulb (OB) by quantitative histochemistry and immunohistochemistry. The highest concentration of G6PD, P450R, and GR was observed in the olfactory nerve layer (ONL), suggesting a correlation in the expression of these enzymes at the gene level. Correlation in staining intensity between G6PD and NADPH-d activities occurred only in part of the ONL, some glomeruli, and scattered periglomerular cells. This peculiar distribution of NADPH-d could reflect a spatial patterning of the nose to bulb projections. Taken together, these results indicate that G6PD expression in the ONL could be related to the importance of generating a substantial supply of NADPH to sustain the detoxifying systems represented by GR and P450R reactions and, only in discrete zones, by NADPH-d activity.
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PMID:Glucose-6-phosphate dehydrogenase and NADPH-consuming enzymes in the rat olfactory bulb. 1579 31

The effect of actinomycin D on the synthesis of the photosynthetic apparatus during illumination of etiolated leaves of Phaseolus vulgaris was studied. The increase of chlorophyll content and of the activities of some photosynthetic enzymes (NADPH diaphorase, ferredoxin, NADP(+) glyceraldehyde-3-phosphate dehydrogenase) was compared with simultaneous measurements of the level of other enzymes not considered associated with photosynthesis (ornithine transcarbamylase, glucose-6-phosphate dehydrogenase, NAD(+) glyceraldehyde-3-phosphate dehydrogenase).The effect of the inhibitor on the synthesis of the components of the photosynthetic apparatus is much larger than its effect on the synthesis of non-photosynthetic enzymes when the antibiotic is supplied 2 hr before illumination. The same selective action is also obtained if actinomycin D is added after 20 hr of exposure of the leaves to light.The markedly different sensitivity to the inhibitor of the synthesis of photosynthetic enzymes, as compared to non-photosynthetic ones, is interpreted as a selective inhibition at the level of DNA-directed synthesis of RNA molecules.This RNA may be involved either in the regulation of chloroplast differentiation or in the specification of some component essential for the formation of the plastidial structure or for the activity of plastidial ribosomes.
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PMID:Selective Inhibition by Actinomycin D of the Synthesis in Photosynthetic and Non-photosynthetic Enzymes During the Greening of Etiolated Bean Leaves. 1665 39

The aim of the study was the estimation of structural and metabolic changes in histaminergic neurons of rat hypothalamic E2 nucleus induced by total external bile drainage. The investigation was carried out on male Wistar rats (n=45). The control group comprised the sham-operated animals, in which the physiological bile drainage was preserved during the whole experimental period. Quantitative histological and histochemical methods were used. In serial frontal cryostat sections of posterior hypothalamus, the activity of the following enzymes was demonstrated histochemically: monoamine oxidase B, succinate dehydrogenase, NADH- dehydrogenase, NADPH-dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and acid phosphatase. Morphometric study of histaminergic neurons was performed in thionin-stained sections. It was found that total external bile drainage resulted in a temporary reduction of the sizes and rounding of neuronal perikarya. Metabolic changes were detected already after 1 day of bile loss, and they were found to progress henceforth. All the pathways of energy metabolism were suppressed, while the acid phosphatase activity was increased, on day 5.
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PMID:[Structural and metabolic changes in the rat hypothalamic histaminergic neurons induced by the bile loss]. 1841 18

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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