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:1.6.99.1 (NADPH-diaphorase)
3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

alpha-Glycerophosphate oxidase, in a strain of Streptococcus faecium, was found to be adaptive to aerated conditions of growth. The enzyme was purified and found to mediate electron transfer from alpha-glycerophosphate to O(2), with the production of stoichiometric concentrations of H(2)O(2) and dihydroxyacetone phosphate. The enzyme is an anionic flavoprotein, with flavine adenine dinucleotide as the apparent prosthetic group. By manometric methods, a K(m) of 6 x 10(-3)m, with reference to substrate concentration, was obtained. An active reduced nicotinamide adenine dinucleotide diaphorase was closely associated with this enzyme in chromatographic mobility on ECTEOLA-cellulose. The purified alpha-glycerophosphate oxidase was not inhibited by KCN, azide, or sulfhydryl reagents, nor was it stimulated by alpha-lipoate, yeast extract, or other supplements.
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PMID:Alpha-glycerophosphate oxidase in Streptococcus faecium F 24. 578 98

Certain neurons in the brain are specifically and intensely stained by a histochemical method which demonstrates nicotinamide adenine dinucleotide phosphate NADPH-diaphorase activity. The cell types containing this enzyme in certain areas of the rat forebrain were examined by combining NADPH-diaphorase histochemistry with the indirect immunofluorescence technique. Neurons containing somatostatin- or avian pancreatic polypeptide (APP)-like immunoreactivities were found throughout the forebrain including the striatum and neocortex. These two neuropeptides were also found to coexist in many telencephalic neurons. After photography, the sections processed for immunohistochemistry were stained for NADPH-diaphorase activity by a histochemical method. It was found that within the striatum all of the neurons that were selectively stained by this technique also contained both somatostatin- and APP-like immunoreactivities. Also in the neocortex NADPH-diaphorase was found only in those neurons displaying somatostatin- or APP-like immunoreactivity. In other brain regions such as the nucleus laterodorsalis tegmenti, NADPH-diaphorase-containing cells did not contain these neuropeptides. The results indicate that NADPH-diaphorase histochemistry provides a simple, reliable, histochemical method to demonstrate those striatal neurons in which somatostatin- and APP-like immunoreactivities coexist. The selective occurrence of this enzyme within these neurons may provide a useful target for pharmacological studies of these neuropeptide-containing cells.
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PMID:NADPH-diaphorase: a selective histochemical marker for striatal neurons containing both somatostatin- and avian pancreatic polypeptide (APP)-like immunoreactivities. 613 31

Striatal neurons containing both somatostatin- and avian pancreatic polypeptide (APP)-like immunoreactivities have been shown to be selectively stained by the histochemical method for nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase activity. In the present study, we have utilized this histochemical technique to examine the morphology of these striatal neurons at the light and electron microscopic levels. Our results indicate that the striatal somatostatin/APP/NADPH-diaphorase neurons occur throughout the striatum and have long, aspiny dendrites, oval, invaginated nuclei with prominent nucleoli, and receive few axosomatic contacts. These cells appear to correspond to a population of medium-sized aspiny interneurons reported previously in Golgi and electron microscopic studies of the striatum.
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PMID:Striatal neurons containing both somatostatin- and avian pancreatic polypeptide (APP)-like immunoreactivities and NADPH-diaphorase activity: a light and electron microscopic study. 613 32

A single administration of chlorophos (trichlorophon) solution (600 mg/kg) (LD50) results in vacuolar distrophy appearing in the white rat liver and is especially pronounced in 2-4 days. Thirty minutes after the poisonous chemical is administered, butyrilcholinesterase (BChE) activity is inhibited by 90%, somewhat later oxidation-reduction enzymes activity decreases and alkaline phosphatase (APh) activity increases. Cytoplasm of hepatocytes is filled with glycogene and nearly deprived of RNA. Owing to the cytophotometric analysis of the enzymatic activity and the stereologic morphometry method, it has been possible to reveal a certain synchronism in the development of distrophic processes, in a decreasing activity of the oxidation-reduction enzymes and in a disturbed synthesis of glycogene and RNA. On the 6th day after chlorophos has been administered, succinate dehydrogenase and nicotinamide-adenine-dinucleotide-phosphate-diaphorase activity, as well as contents and distribution of RNA in hepatocytes reach their control values. BChE and APh activity does not restore. During the whole experiment there is not any statistically significant change in the volumetric part of the sinusoid capillaries and in the stellate reticuloendotheliocytes. Thus, the main effect of chlorophos action is a specific inhibition of ChE, that results in certain structural changes and in changes of the histoenzymatic parameters of the liver.
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PMID:[Morpho-functional changes in the liver after exposure to cholinesterase inhibitors]. 619 75

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
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PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

Crude extracts of Methanospirillum hungatei strain GP1 contained NADH and NADPH diaphorase activities. After a 483-fold purification of the NADH diaphorase the enzyme was further separated from contaminating proteins by polyacrylamide disc gel electrophoresis. Two distinct activity bands were extracted from the acrylamide, each one having oxygen, 2,6-dichlorophenolindophenol, and cytochrome c linked activities. In these preparations NADPH could not replace NADH as electron donor. During the initial purification steps all activity was lost due to the removal of a readily released cofactor. Enzyme activity was restored by either FAD or a FAD fraction isolated from M. hungatei. Oxidase activity exhibited a broad pH optimum from 7.0 to 8.5 and apparent Km values of 26 microM for NADH and 0.2 microM for FAD. Superoxide anion, formed in the presence of oxygen, accounted for all of the NADH consumed in the reaction. The molecular weight of the diaphorase was about 117 500 by sodium dodecyl sulfate gel electrophoresis. Sulfhydryl reagents and chelating agents were inhibitory. Inactivation, which occurred during storage in phosphate buffer at 4 degrees C, was delayed by dithiothreitol. The isolated NADH diaphorase lacked NADPH:NAD transhydrogenase and NAD reductase activities.
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PMID:Isolation and characterization of a FAD-dependent NADH diaphorase from Methanospirillum hungatei strain GP1. 626 28

Changes in the activity of 13 enzymes are described in the process of cytodifferentiation of the nerve cells of spinal ganglion, the motor neurons of spinal cord and large nerve cells of the III layer of tectum opticum in 7, 10 and 21 day old chick embryos. Cytophotometry was performed with MZFV-1 (LOMO) by means of plug-method. A relatively high activity of glucose-6-phosphat dehydrogenase, diaphorase, alpha-glycerophosphate dehydrogenase and, partially, acetylcholine esterase was found already in the 7 days old embryo. The activity of monoamine oxidase, aldolase-glyceroaldehyde phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase increased markedly on the 21st day. When studying the reciprocal distribution of two enzymes in separate cells, pairs of enzymes with a high value of correlation coefficient were found. The cytodifferentiation was found to be accompanied by changes in the coefficient of correlation of the same pair of enzymes.
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PMID:[Enzymes in the process of neuronal differentiation of the hen spinal ganglion, spinal cord and tectum opticum. A cytophotometric histochemical study]. 683 47

Morphological and histochemical investigations of the activity of succinate, malate, lactate, isocitrate, and glucoso-6-phosphate dehydrogenases, and NAD-diaphorase in the central, marginal, borderline and perifocal zones of ischemic brain infarctions were carried out. Deep changes in the activity of the enzymes listed, and peculiarities of this activity in various brain structures and tissues were revealed. A connection between the activity of the enzymes, the duration of the infarction, and the structural and biochemical peculiarities of the affected brain part is demonstrated. A suggestion is made on the pathogenesis of the ischemic infarctions and on the possibility of using histochemical data for the purposes of the pathoanatomic diagnosis.
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PMID:[Morphologo-histochemical characteristics of ischemic cerebral infarcts in the acute stage of the stroke in patients with atherosclerosis]. 689 83

We describe two fully enzymic methods, fluorometric and colorimetric, for determination of triglycerides (triacylglycerols) in serum. Samples are incubated with microbial lipase for 10 min, and the glycerol released from the triglycerides is oxidized by NAD+ in the presence of glycerol dehydrogenase. In the fluorometric method, the resulting NADH is in turn oxidized by resazurin as catalyzed by diaphorase to form resorufin, a highly fluorescent compound. In the colorimetric method, the NADH is oxidized by coupling with a tetrazolium salt/diaphorase system to form formazan, a highly colored compound. Calibration curves, constructed by plotting change in fluorescence or absorbance vs concentration of triglycerides, were linear up to 6 and 5 g of triglycerides per liter of serum for the fluorometric and colorimetric methods, respectively. The assays require only 5 and 15 microL of serum for fluorometry and colorimetry, respectively. The CV was 0.59% for the fluorometric method, 0.91% for the colorimetric procedure. The time for analysis for either method is less than 15 min. The results correlate well with those obtained by the Dow Diagnostic Kit method, a colorimetric method in which glycerol kinase and glycerol-1-phosphate dehydrogenase form NADH from ATP and NAD+ in the presence of glycerol and glycerol 1-phosphate.
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PMID:Fluorometric and colorimetric enzymic determination of triglycerides (triacylglycerols) in serum. 689 89

The quantitative cytochemical investigation of the prodigiozan effect on the enzymatic activity of the peritoneal macrophages was performed on mice. The drug was administered in a single dose of 150 microgram/kg 24 hours before the specimen collection. Prodigiozan promoted a reliable increase in the activity of the enzymes participating in glycolysis (lactate and cytoplasmic alpha-glycerophosphate dehydrogenases), hexoso-monophosphatic pathway of glucose oxidation (glucoso-6-phosphate dehydrogenase), succinate dehydrogenase, NADP. N-diaphorase and lysosomal enzymes, such as acid phosphatase and non-specific alpha-naphthyl acetate esterase. The changes indicate that activation of the macrophages is one of the significant mechanisms of increasing the host nonspecific resistance with prodigiozan.
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PMID:[Prodigiozan as an activator of peritoneal macrophages]. 727 Dec 60


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