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 authors investigated the dehydrogenase histochemistry of arterioles on 22 muscular biopsies from 14 male and 8 female patients with different clinical forms of atherosclerosis, and in 5 controls. There was a diminution with age of all the enzymes studied. In 3 of 6 cases with pathological lesions (thickening of endothelium, fragmentation of the internal elastic lamina, thrombosis) there was a regional diminution of NADH-diaphorase and NADPH-diaphorase activities parallel with an increase of the reaction for lactic dehydrogenase and glutamate dehydrogenase in the muscular cells and endothelium.
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PMID:Histoenzymology of muscular arterioles. 81 50

The fungicide dexon (p-dimethylaminobenzenediazosulfonate, Na-salt) inhibits the NADH oxidase activity of submitochondrial particles (ETP) from beef heart (semi-inhibition concentration 1.4 muM), while the succinate oxidase activity is unaffected. Measurements of the activity of several enzymatic partial reactions of the respiratory chain of ETP suggest that dexon acts directly on the flavine of NADH dehydrogenase. Soluble NADH-cytochrome c-oxidoreductase (MAHLER) and rotenone-insensitive NADH ubiquinone reductase are also inhibited by dexon. At low concentrations of dexon, inhibition of ETP starts slowly only after addition of NADH. Preincubation without NADH increases the amount of inhibition, but does not prevent the time delay. It is assumed that an electron flux through the respiratory chain, or reduction of flavine is prerequisite for the reaction of dexon with the action site. Furthermore, dexon inhibits the NADH dehydrogenase located at the outer surface of the inner membrane of plant mitochondria, accessible to extramitochondrial NADH and insensitive to rotenone, as has been shown on isolated mitochondria from cauliflower (Brassica oleracea L). In addition, dexon inhibits selectively the NADH dehydrogenase of the DT diaphorase (ERNSTER) from rat liver cytosol. In contrast, the dicoumarol-insensitive NADH dehydrogenase (ZINSMEYER et al.) from rat liver cytosol, the NADH-cytochrome b5-reductase (STRITTMATTER) from rat liver microsomes, the rotenone-insensitive NADH-cytochrome c-oxidoreductase of the outer membrane of rat liver mitochondria, soluble NADH-oxidase from Escherichia coli, and NADH-dehydrogenase from human erythrocytes are not inhibited. The results suggest that dexon is a group reagent to certain pyridine nucleotide-dependent flavine enzymes.
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PMID:[Action of the systemic fungicide dexon on several NADH dehydrogenases]. 82 48

The use of a low pressure perfusion method for enzyme histochemical reactions in the cochlea of guinea pig is proved in the case of the demonstration of the NADH-diaphorase. It was shown by measuring of the microphonic potentials during the perfusion, that the perfusion medias caused practically no chemical or mechanical defections of the hair cells under the new conditions of working. The activities of the NADH-diaphorase were demonstrated mainly in the hair cells and in the nervous fibres of the organ of Corti. A remarkable NADH-diaphorase activity was detected in the Boettcher cells too.
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PMID:[A low pressure perfusion method suitable for enzyme histochemical studies on the cochlea exemplified with the demonstration of NADH-diaphorase activity (author's transl)]. 82 79

In order to localize 3beta-hydroxysteriod dehydrogenase activity on the ultrastructural level, sections of Newt and Rat adrenocortical tissues, fixed in a mixture of glutaraldehyde (0.25%) and formaldehyde (1%), were incubated in a medium containing namely a 3beta-hydroxysteroid as substrate, NAD, potassium ferricyanide as final electron acceptor and copper sulfate. In some experiments, phenazine methosulfate (PMS), an electron carrier which can substitute for the activity of the endogenous NADH-diaphorase, is added at various concentrations to the incubation medium. A final precipitate of copper ferrocyanide is observed in the immediate vicinity of the tubules of the smooth endoplasmic reticulum, or in contact with their external faces. The reaction product can also be seen in mitochondrial cristae. The reaction does not take place in incubation media lacking substrate or containing cyanoketone, a specific inhibitor of 3beta-hydroxysteroid dehydrogenase. the addition of PMS to the incubation medium increases the intensity of the reaction, but does not modify the localization of the precipitate.
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PMID:Ultracytochemical demonstration and probable localization of 3beta-hydroxysteroid dehydrogenase activity with a ferricyanide technique. 83 7

Methyl-GAG was tested in organotypic cultures of malignant tumors of human and mice. In 3 cases, a reduction of the activity of two oxydoreductases (lactate dehydrogenase and NADH-diaphorase) after treatment with methyl-GAG was observed whereas in 19 other cultivated tumors no change of enzyme activity was induced by methyl-GAG. Electronmicroscopy revealed only minor structural alterations of tumor cells after application of methyl-GAG as compared with control cultures.
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PMID:[Histochemical and ultrastructural investigations on the activity of methylglyoxal (bis)-guanylhydrozan (methyl-GAG) on organ cultures of malignant tumors (author's transl)]. 86 71

Sheep erythrocyte membranes have been shown in this laboratory to undergo spontaneous vesiculation when incubated at 4 degrees, fractionating into two bands in dextran gradients (R. McGuire and R. Barber, submitted for publication). While vesicles were observed to be formed in several solvent systems, incubation in the presence of complexors to remove divalent cations was found to be the most efficient method for both vesicle formation and their detachment from the residual membrane. We report here on the characterization of these vesicles formed by spontaneous vesiculation. In the presence of a hypotnoic buffer containing 1 mM EDTA, vesicle production proceeds linearly up to 50 hours and declines, reaching its maximum at 72 hours with up to 20% of the total membrane protein found in the upper band. This upper band is shown in electron micrographs to be composed chiefly of closed vesicles, while the particles in the lower band appear morphologically similar to the original ghosts. Total phospholipid phosphorus and cholesterol in the vesicles are enriched to the same extent, giving a lipid to protein ratio of 2 times that found for whole ghosts. The vesicles contain the same individual phospholipids as the ghosts. The protein composition of these vesicles is unique, in that they are almost depleted in the known extrinsic membrane proteins, while containing practically all types of the various glycoproteins of the original membrane. The two main intrinsic membrane proteins (with apparent molecular weights of 160,000 and 100,000) are found almost exclusively in the vesicles, virtually depleted in the residual ghost-like particles. The protein with 160,000 molecular weight is shown here to be a glycoprotein, giving an anomalous molecular weight on sodium dodecyl sulfate gels and having a molecular weight of approximately 50,000 after lipid extraction. This same glycoprotein appears to fractionate with acetylcholinesterase. From the accessibilities of the substrates to the membrane acetylcholinesterase and NADH-diaphorase, it is concluded that the vesicles are right-side-out and sealed to small molecules. There are more membrane sialic acid residues accessible to neuraminidase in the vesicles (in terms of number of residues/mg og membrane protein) than in ghosts, further supporting the conclustion that these vesicles have a normal orientation and are enriched in glycoproteins. The specific activity of acetylcholinesterase in the vesicles is increased 5- to 6-fold over that found in the original ghosts and almost 20-fold over that in the residual ghost-like particles. Consequently, spontaneous vesiculation occurs simultaneously with the enrichement of specific membrane proteins in certain regions of the lipid bilayer. It is postulated that these domains in the membrane, containing clusters of specific intrinsic membrane proteins, bud out and subsequently release glycoprotein-enriched lipid vesicles.
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PMID:Glycoprotein-enriched vesicles from sheep erythrocyte ghosts obtained by spontaneous vesiculation. 93 96

In rats given 15% solution of ethyl alcohol (v/v) instead of drinking water adlibitum for eight months, histochemical analysis showed a dictinct fall in activities of the oxidative enzymes (succinate and lactate dehydrogenases, DPNH-diaphorase) in the centro-acinar cells of the pancreas and in the islets of Langerhans.
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PMID:Chronic alcoholism and the pancreas. 103 49

The levels of acetylcholine and choline were measured in various brain regions of the rat after fixation by microwave irradiation of the head and after decapitation and subsequent freezing in liquid nitrogen. Levels of acetylcholine were increased by approximately 50% after microwave irradiation, while choline levels were reduced. These biochemical findings were correlated with virtually complex loss of acetylcholinesterase and NADH-diaphorase activity after 1 s exposure to microwave irradiation at a level of 5 kW.
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PMID:Fast fixation of brain in situ by high intensity microwave irradiation: application to neurochemical studies. 104 75

The activity of succinatedehydrogenase, mitochondrial alpha-glycerophosphatedehydrogenase and NADH2-diaphorase was studied cytochemically and histochemically in the myocardium and lymphocytes of rats and mice after the effect of hypoxia in a hyperbaric chamber. A short-duration effect of hypoxia and step-wise adaptation during a month was shown to result in a growing activity of the enzymes both in the lymphocytes and in the myocardium. Hypoxia during a month and readaptation during the same period caused a monotonous decrease of the activity of dehydrogenases. The conducted analysis permitted to reveal a distinct correlation between the activity of dehydrogenases in the lymphocytes and in the myocardium. The authors emphasize the similarity of the changes in the activity of the enzymes in the lymphocytes and in the myocardium.
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PMID:[Activity of the dehydrogenases of the myocardium and lymphocytes in experimental hypoxia]. 115 23

Infusion of 1 mul arachis oil containing 1.5 mug bis-(1 -methylethyl)phosphorofluoridate (di-isopropylfluorophosphate: DFP) into the caudate--putamen nucleus and substantia nigra of rats produced a considerable reduction of histochemical staining for acetylcholinesterase (AChE) in these two brain regions 30--120 min after injection. Thereafter, regeneration of AChE occurred within the zone of DFP effect. These new stores of AChE were associated with discrete neuronal perikarya and their processes. Intracerebral DFP administration had little or no histochemically detectable effect on NADH-diaphorase. Thionin staining was similarly unaffected. The results with punctate intracerebral application of DFP were replicated by intramuscular injection of 1.5 mg/kg DFP. Although the significance of dopaminergic--cholinergic interactions in the neostriatum could not be elucidated on the basis of these histochemical data, the thesis was advanced that dopamine neurons in the pars compacta of the substantia nigra also contained AChE, possibly to inactivate acetylcholine released from cholinergic fibers afferent to this neural structure.
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PMID:Acetylcholinesterase-containing neurons in the neostriatum and substantia nigra revealed after punctate intracerebral injection of di-isopropylfluorophosphate. 123 57


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