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)

Optochin-resistant mutant and wild-type diaphorases were purified approximately 300-fold by a combination of batch adsorption and column chromatography with diethylaminoethyl cellulose, and were characterized with regard to their pH optima, sensitivity to optochin inhibition and heat inactivation, Michaelis constants with flavine mononucleotide (FMN) and reduced nicotinamide adenine dinucleotide (NADH), and inhibition constants with optochin hydrochloride. The pH optima of the purified diaphorases were similar, but the purified diaphorases from the optochin-resistant strains were approximately four to five times more resistant to heat inactivation at 45 C than was the wild-type diaphorase. Purified diaphorase preparations from the optochin-resistant pneumococci had greater activities per milligram of protein and were more resistant to optochin inhibition than the preparation from the optochin-sensitive pneumococcus. Michaelis constants for FMN and NADH were similar; however, the inhibition constants of the optochin-resistant diaphorases were four to eight times greater than that of the optochin-sensitive diaphorase. Optochin hydrochloride produced a noncompetitive type of inhibition with FMN as substrate but a competitive type of inhibition with NADH as substrate. Optochin hydrochloride produced an approximately 10-fold increase in the Michaelis constant for NADH. The concentration of drug required to produce this effect was, however, greater with the mutant diaphorases than with the wild-type diaphorase. Optochin hydrochloride quenched the fluorescence of riboflavine. This phenomenon did not appear to be related to the diaphorase-inhibitory activity of the drug, however, since the pH requirements of the two reactions were different. Quenching of riboflavine fluorescence by optochin hydrochloride increased with a rise in pH, whereas inhibition of diaphorase activity by optochin hydrochloride was greater at pH 6.8 than at pH 7.6.
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PMID:Purification and properties of mutant and wild-type diaphorases from Diplococcus pneumoniae. 438 90

A slow-growing mutant of Escherichia coli with greatly elevated nicotinamide adenine dinucleotide phosphate (reduced; NADPH) oxidase activity has been isolated. The oxidase activity of the wild-type organism, normally low at pH 7.5, was increased when the assay was performed at pH 6.0. Sucrose density gradients of sonic extracts of the mutant and wild-type strains revealed several peaks of NADPH oxidase activity at pH 6.0. The parent organism had a peak of activity of high molecular weight which was absent from the mutant. The mutant strain had an activator capable of increasing the activity of all wild-type density gradient peaks, especially the one of high molecular weight. The activator was either missing or masked in the wild type. Agar gel electrophoresis of the extracts uncovered a rapidly moving band from the wild type, missing from the mutant; the material in this band had weak NADPH-diaphorase activity and strongly inhibited the activity of the mutant NADPH oxidase. It was concluded that, in wild-type E. coli, NADPH oxidase activity is regulated by a proper balance of an activator and an inhibitor. The absence of the inhibitor, as in the mutant, or the inactivation of the inhibitor at acid pH levels, results in a high level of NADPH oxidase activity. The relation of high NADPH oxidase levels and subsequent decrease of the NADPH pool to the decrease in growth rate is considered.
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PMID:Escherichia coli mutant with elevated nicotinamide adenine dinucleotide phosphate (reduced) oxidase activity. 438 86

Evidence that the bactericidal ability and the stimulated oxidative metabolism of leukocytes appear in parallel during fetal development of the Minnesota Miniature pig has been obtained by application of the techniques applied to studies of human cells. It was demonstrated that leukocytes from 87- to 90-day fetuses were fully capable of ingesting Staphylococcus aureus but greatly diminished in bactericidal capacity as compared to leukocytes of older fetuses and adults. Although resting levels of oxygen consumption and hexose monophosphate pathway activity of leukocytes from the younger fetuses compared well with those of leukocytes from older animals, the phagocytosis-stimulated increments of metabolism were much less at 87 to 90 days of gestation than at later developmental stages. Both bactericidal capacity and increased metabolism of leukocytes reach adult levels by 100 days of gestation (normal gestation period of 115 to 120 days). Acrylamide gels stained for reduced nicotinamide adenine dinucleotide (NADH) and NADH phosphate (NADPH) diaphorase activity after disc electrophoresis of leukocyte extracts revealed normal mobility and intensity of NADH diaphorase bands. Three NADPH diaphorase bands were present in adult leukocyte extracts. Only the fast-migrating NADPH diaphorase band of 87- to 90-day cells stained with decreased intensity. This "deficiency" was no longer present at the later fetal period. The fast-migrating NADPH diaphorase band may represent an electron transfer protein which functions in cyanide-insensitive respiration of the leukocytes of the pig.
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PMID:Development of bactericidal capacity and phagocytosis-associated metabolism of fetal pig leukocytes. 463

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

Experiments were performed to determine whether conditions which cause the rapid loss of nitrate reductase activity in Neurospora crassa mycelia were accompanied by the loss of antigenically detectable nitrate reductase protein. When mycelia with nitrate reductase activity were transferred to ammonia media, there was a rapid loss in the reduced nicotinamide adenine dinucleotide-nitrate reductase activity plus the parallel loss of the reduced nicotinamide adenine dinucleotide-diaphorase and the reduced methyl viologen-nitrate reductase activities associated with the nitrate reductase. In addition, there was the loss of cross-reacting material to anti-nitrate reductase antisera that was concomitant with the loss of nitrate reductase activity. When mycelia were exposed to either ammonia plus cycloheximide, nitrate plus cycloheximide, or nitrogen-free media, or to media which lacked an assimilable carbon source, the amount of cross-reacting material declined in concert with the nitrate reductase activity. The mutant nit-6, which lacks nitrite reductase activity, was exposed to ammonia or nitrate plus cycloheximide media. The nitrate reductase and the amount of cross-reacting material declined together as in the wild-type mycelia. We conclude that the loss of nitrate reductase activity was accompanied by the specific loss of this protein and that no pool of inactivated nitrate reductase molecules existed.
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PMID:Repression of nitrate reductase activity and loss of antigenically detectable protein in Neurospora crassa. 644 48

A comparison was made of muscle from two locations in both the longissimus and the semitendinous muscles of normal and malignant hyperthermia-susceptible swine. Serial frozen sections were stained for alkali-stable adenosine triphosphatase (ATPase), phosphorylase, and the oxidative enzymes succinate dehydrogenase and reduced nicotinamide adenine dinucleotide (NADH)-diaphorase. Myofiber types were identified on the basis of these staining reactions. There was no consistent statistically significant difference between muscle from normal and muscle from susceptible swine with any system of fiber classification. This is contrary to several published reports but consistent with physiologic studies which indicate that both oxidative and glycolytic pathways are abnormally active during the onset of malignant hyperthermia.
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PMID:Histochemical observations on muscle from normal and malignant hyperthermia-susceptible swine. 644 66

The profiles of fiber types in hindlimb muscles from the tree shrew (Tupaia glis), lesser bushbaby (Galago senegalensis), and the slow loris (Nycticebus coucang) were determined using histochemical techniques. Fibers were classified as fast-twitch oxidative-glycolytic (FOG), fast-twitch glycolytic (FG), slow-twitch oxidative (SO), or fast-twitch oxidative (FO), according to reactions for alkaline-stable ATPase, acid-stable ATPase, alpha-glucan phosphorylase, reduced nicotinamide adenine dinucleotide diaphorase, succinate dehydrogenase, mitochondrial alpha-glycerophosphate dehydrogenase (MaGPDH), and beta-hydroxybutyric dehydrogenase, as well as glycogen staining by the periodic acid-Schiff technique. Prolonged dissection of numerous muscles was carried out on hindlimbs submersed in cold Tyrode's solution; such treatment had no qualitative effect on enzyme staining reactions, but it is not a suitable procedure if one wishes to stain for glycogen. Fast-twitch oxidative (FO) fibers are alkaline-stable ATPase-positive and possess low MalphaGPDH enzyme activity. These fibers have not been reported previously in any hindlimb muscles. No muscles of any species studies were homogeneous with respect to fiber type. Slow loris muscles lacked FG fibers. The majority of the muscles of the slow loris contained numerous SO fibers. The relationship between enzyme activities and locomotor pattern is discussed.
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PMID:Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types. 645 15


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