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:1.6.5.2 (NQO1)
6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

This study shows a marked increase in the activity of the soluble enzyme DT-diaphorase and of the histochemical activity of the reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate nitroblue tetrazolium menadione-mediated reductases in human colonic carcinomas when compared with the enzymatic activities of portions of the colon uninvolved by the carcinomatous process. The activity of the reductases in histological sections was quantitated with a microphotometer. It is believed that the increase in histochemical nitroblue-tetrazolium reductase activity in the histochemical reactions in colonic carcinomas is a real reflection of the activity of the DT-diaphorase, because the increase in the dehydrogenation of reduced nicotinamide adenine dinucleotide equals the dehydrogenation of reduced nicotinamide adenine dinucleotide phosphate when measured biochemically in the soluble fraction, or histochemically, by microspectophotometry in tissue sections; meanwhile, the biochemical dehydrogenation of NAD(P)H by the particulate fractions shows that the enzymatic activities are not altered by the neoplastic process. The biological significance of these changes is discussed in the text.
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PMID:Biochemical and quantitative histochemical study of reduced pyridine nucleotide dehydrogenation by human colonic carcinomas. 630 79

The mechanisms by which 2(3)-tert-butyl-4-hydroxyanisole (BHA) protects against chemical carcinogenesis and toxicity include enhancement of the activities of several detoxification enzymes. In previous studies, 14-day administration of BHA to female CD-1 mice at 0.75% of the diet led to large increases in cytosolic glutathione transferase (EC 2.5.1.18) and reduced nicotinamide adenine dinucleotide (phosphate) dehydrogenase (quinone) (EC 1.6.99.2) [NAD(P)H:quinone reductase; DT-diaphorase] specific activities in several tissues, and elevated hepatic glutathione transferase messenger RNA. In the present study, one day of dietary BHA significantly increased NAD(P)H:quinone reductase and glutathione transferase activities in the liver, kidney, and proximal small intestine, and NAD(P)H:quinone reductase activity in the forestomach and lung. In the proximal small intestine, glutathione transferase specific activities toward 1-chloro-2,4-dinitrobenzene and 1,2-dichloro-4-nitrobenzene rose to 2.6 and 8 times those of control, respectively, and NAD(P)H:quinone reductase specific activity doubled, within 1 day on the BHA diet. Six hr after a single p.o. dose of BHA (620 mg/kg), intestinal glutathione transferase specific activities were 30 to 50% above those of control mice. In liver, the kinetics of increase of glutathione transferase messenger RNA were in accord with increased synthesis as the mechanism of elevation of glutathione transferase activity in response to BHA. Although changes in mixed-function oxygenase activities have been reported to occur more rapidly, the kinetics of the response of glutathione transferase and NAD(P)H:quinone reductase specific activities to BHA indicates that nonoxidative detoxification potential is substantially enhanced within 24 hr or less after initiation of BHA administration.
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PMID:Kinetics of glutathione transferase, glutathione transferase messenger RNA, and reduced nicotinamide adenine dinucleotide (phosphate):quinone reductase induction by 2(3)-tert-butyl-4-hydroxyanisole in mice. 643 66

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 vitamin K-dependent carboxylase extracted from rat liver microsomes by 3-([3-cholamidopropyl] dimethylammoniol)-1-propane sulfonate detergent solution has been partially purified by chromatography on Ultrogel AcA-34 followed by carboxymethyl-Sepharose chromatography and pentapeptide affinity chromatography. The carboxylase appears to be composed of two proteins, the enzyme and endogenous substrate as judged by the incorporation of 14CO2 into trichloroacetic acid insoluble protein. The apparent Km for Phe-Leu-Glu-Glu-Leu as carboxylation substrate is approximately 3 mM. 2,3,5,6-Tetrachloro-4-pyridinol at 10 microM inhibits 90% of the enzyme activity, whereas maximal stimulation (1.7-fold) by pyridoxal 5'-phosphate is obtained at 1 mM and by Mn2+ at 5 mM. The stimulation by pyridoxal 5'-phosphate and by Mn2+ are not additive. The carboxylation of Phe-Leu-Glu-Glu-Leu at 20 degrees C is linear for 90 min. Vitamin K1 plus NADH do not replace vitamin K1 hydroquinone, indicating that vitamin K reductase is not part of this purified carboxylase-substrate complex. Vitamin K epoxidase activity co-elutes with the carboxylase complex. Some 400-fold purification from microsomes has been obtained to yield enzyme preparations with a specific activity of approximately 17,000 pmol of CO2 fixed into peptide/mg of enzyme protein, which is some 15-fold greater than any previously reported enzyme preparation from rat liver microsomes.
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PMID:Vitamin K-dependent carboxylase. Partial purification and properties of the enzyme-substrate complex. 717 81

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

Nitric oxide synthase-like immunoreactivity was found in a subpopulation of sympathetic postganglionic neurons in the cat stellate and lower lumbar ganglia. In the ganglia of other segments such cells were rare. Double staining for tyrosine hydroxylase-like immunoreactivity and nitric oxide synthase-like immunoreactivity or the reduced nicotinamide adenine dinucleotide phosphate diaphorase reaction indicated that nitric oxide synthase-like immunoreactivity and reduced nicotinamide adenine dinucleotide phosphate diaphorase reactivity was always co-localized and was confined to tyrosine hydroxylase-negative (presumably cholinergic) ganglion cells, and was present in most of them. The occurrence of nitric oxide synthase in two subpopulations of cholinergic postganglionic neurons was investigated in triple staining experiments. Presumptive sudomotor neurons have been previously defined as scattered cells containing calcitonin gene-related peptide-like immunoreactivity, usually accompanied by vasoactive intestinal peptide-like immunoreactivity: 99% of these contained nitric oxide synthase. Presumptive muscle vasodilator neurons have been previously identified as clumped cells with strong vasoactive intestinal peptide-like immunoreactivity but no calcitonin gene-related peptide-like immunoreactivity: 70% of these contained nitric oxide synthase. Sweat glands were found in the paw pad skin surrounded by varicose fibres showing calcitonin gene-related peptide-like immunoreactivity and vasoactive intestinal peptide-like immunoreactivity, confirming previous work. Such fibres also stained for nitric oxide synthase-like immunoreactivity and reduced nicotinamide adenine dinucleotide phosphate diaphorase reactivity, although their staining was relatively weaker than in the corresponding cell bodies. Varicose fibres with the same chemical coding were also found around all large and most medium and small arteries in the paw skin as well as around arteriovenous anastomoses. Fibres with the muscle vasodilator coding (vasoactive intestinal peptide-like immunoreactivity without calcitonin gene-related peptide-like immunoreactivity) were not seen in paw skin. These results suggest that nitric oxide may act as a co-transmitter (with acetylcholine, substance P, vasoactive intestinal peptide and calcitonin gene-related peptide) in sudomotor neurons and (with acetylcholine and vasoactive intestinal peptide) in vasodilator neurons. Collateral branches of sudomotor neurons may innervate skin vessels, and release vasodilator transmitters including nitric oxide to cause the vasodilatation which provides the fluid supply for sweat formation. Alternatively, separate vasodilator neurons to skin may share the same chemical code as sudomotor neurons.
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PMID:Nitric oxide synthase and chemical coding in cat sympathetic postganglionic neurons. 747 30


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