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)

The method of visual quantitative estimation was employed to determine the index of enzymes activity in embryonal cells cultures infected with Rous virus. In early terms (1-7 days after infection) a moderate production of diformazane was noted in the presence of glucoso-6-phosphatiosomerase, phosphoglucomutase, pyruvatoxidase, NAD. H2- and NADP. H-2-diaphorase, other enzymes showing no distinquishable deviations in the activity, as compared with the normal culture. In later terms (13-27 days) during the proliferation of the transformed cells there was found an increased level of the glycolysis enzymes activity, pentose cycle, hydrolysis of ortho-phosphoric acid monoethers and reduced lemon acid cycle and tissue respiration. Cytoplasmatic vacuoles formed in the transformed cells seem to represent hypertrophic lysosomes and phagolysosomes.
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PMID:[Quantitative cytochemical detection of enzymes in cultured cells following infection with Rous virus]. 17 56

The distribution of succinic dehydrogenase, (see article), glucose-6-phosphat-dehydrogenase, alkaline and acid phosphatases and glucose-6-phosphatase was studied by means of the incubation of whole cestodes. Succinic dehydrogenase, NAD-diaphorase and glucose-6-phosphatdehydrogenase are connected in general with the fixating apparatus of the scolex and genital organs; phosphatases -- with the integument tissues, excretory system and calcareous corpuscles. The results obtained are in complete agreement with the available data on the distribution of the enzymes studied. The incubation method of whole cestodes can be useful for field works.
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PMID:[Distribution of some enzymes in totally stained preparations of cestodes]. 17 33

Biopsies from vastus lateralis muscle of male patients suffering from chronic ethanol abuse were studied with regard to histochemical reactions of ATPase and NADH-diaphorase; enzymatic activities of triosephosphate dehydrogenase (TPD), lactate dehydrogenase (LD), and cytochrome c oxidase (cytox); content of ATP, creatine phosphate, and glycogen; and volume fractions of fat, mitochondria, and fibrillar and extrafibrillar space. The results were compared with those from controls without known abuse of ethanol. The relative numbers of fibers were the same in two groups, but the size of the fast-twitch-glycolytic (white) fibers was diminished in the alcoholic group. The activities of TPD and LD were diminished in skeletal muscle of the alcoholics. This is most probably caused by the reduced amount of fast-twitch-glycolytic tissue, as there was a good correlation between this amount and the activity of the two enzymes. The activity of cytox was slightly lower in muscle of the alcoholics than in that of the controls. The volume fraction of mitochondria was lower in the alcoholic group than in the control group. Volume fractions of fat and fibrillar and extrafibrillar space were equal in the two groups. No significant differences were found in the amount of glycogen and ATP in the muscle of the two groups. However, the content of creatine phosphate is higher in the alcoholic group than in the control group.
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PMID:Effects of chronic ethanol abuse on structure and enzyme activities of skeletal muscle in man. 17 13

The activity of 8 enzymes (dehydrogenase and diaphorase) in cells of 110 neuroectodermal tumours was studied. The overall assessment showed that the activity of these enzymes varied: the highest was noted for NAD-diaphorase and lactadehydrogenase, the lowest--for enzymes of Krebs' cycle. The activity of dehydrogenase and diaphorase was different in neuroectodermal tumours of different origin. Not infrequently, there was observed "enzymatic polymorphism" of the cells of one and the same tumour. A higher activity of these enzymes in tumour cells, as a rule, correlated with a greater amount of cytoplasma and with a shift to the latter of the nucleo-cytoplasmatic ratio. Metabolism of tumour and reactively hypertrophied astrocytes, as judged by some histochemical findings, showed traits of similarity.
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PMID:[Histochemistry of the oxidation-reduction enzymes in the cells of neuroectodermal tumors]. 17 67

16 cases of goiter were examined for C-cells and 4 cases with normal thyroid gland. C-cells identification was based on masked metachromasia. There was stated both in toxic, atoxic goitrous tissue two forms of C-cells. The first characterized by positive metachromatic reaction and weak argyrophinty, the second type of C-cells were orthochromatic and argyrophilic. Metachromatic C-cells characterized as a rule by high alpha glycero phosphate menadione reductase as well succinic dehydrogenase and cytochrome oxidase.
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PMID:Thyroid C-cells in normal and goitrous gland: a histochemical study. 17 26

A covalently bound adduct of nicotinamide adenine dinucleotide (NAD) with alginic acid has been found to be enzymatically active and to undergo electrochemical oxidation or reduction without significant loss of its enzymatic activity. The preparation of the adduct itself (from NAD+, alginic acid, and 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate) is also accomplished with substantially complete retention of enzymatic activity. This adduct has been converted from the oxidized to the reduced form by controlled potential electrolysis using mercury and stainless-steel electrodes. This electrolytically produced NADH complex could be oxidized again to the enzymatically active NAD+ complex by enzymatic reaction with the proton acceptor, 2,6-dichlorophenol indophenol, as catalyzed by diaphorase. Using this electrolytic method with immobilized NAD, it is now possible to carry out redox reactions in which NADH is enzymatically oxidized to NAD+, with the simultaneous electrolytic regeneration of the reduced form, NADH, from the oxidized form, NAD+, produced in the enzymatic reaction.
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PMID:Electrolytic regeneration of the reduced from the oxidized form of immobilized NAD. 17 64

Thirty extraocular muscles (EOM) from 20 patients were evaluated by light microscopy (LM), electron microscopy (EM), and enzyme histochemistry (EZH). Twenty-one EOM were obtained from 13 patients with strabismus, 9 EOM from 4 patients undergoing eye surgery for other reasons and from 3 autopsy cases. One mum thick sections revealed marked variation in muscle fibre shape and size and in myofibrillar structure; also noted were small, hypertrophied, whorled, and ringbinden fibres. Dense and granular material in the central portion of some fibres and sarcomere disruption in 2--3 mum sections was observed. EZH revealed the absence of the classical mosaic pattern usually found in skeletal muscles. ATPase studies were inconsistent and did not correlate with the expected reciprocal activity of NAD-H diaphorase, particularly on the large fibres. Ultrastructural features consisted of vacuoles within myofilament bundles, "smearing" of Z bands, and "nemaline rods". Occasional myelin figures and lipid-like droplets were observed in subsarcolemmal spaces, associated with scattered clusters of glycogen granules. Abnormal mitochondria and subsarcolemmal inclusions of dense and granular material were conspicuous. "Leptomeric" profiles, "Zebra bodies", or "striated bodies" were noted in 8 EOM's, and an Hirano body was found in 1. The intramuscular nerves contained structures resembling "Luse bodies" in 7 cases. These observations suggest that EOM from individuals with and without strabismus possess unique structural characteristics suggestive of developmental and morphological disarrangement of contractile elements. Some of these changes might play a role in the pathogenesis of strabismus and in the development of clinical symptoms. These features are significantly different from striated skeletal muscle. Therefore the criteria used in the pathological evaluation and diagnosis of skeletal muscle disorders cannot be unequivocally applied to EOM investigations. These data establish the necessity to determine histological norms, ultrastructural patterns, and develop new enzyme histochemistry criteria for the evaluation of EOM. Only then can an acceptable comparison of EOM and skeletal muscle be made.
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PMID:Extraocular muscles: light microscopy and ultrastructural features. 17 43

Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have been obtained in homogeneous state from asparagus mitochondria. They are flavin enzymes with 1 mol of FAD/mol of protein. Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have s20,w of 6.22 S, 6.39 S, and 5.91 S, respectively, and molecular weights of 111,000, 110,000, and 95,000 (sedimentation equilibrium) or 112,000, 112,000, and 92,000 (gel filtration). They are slightly acidic proteins with isoelectric points of 6.75, 5.75, and 6.80. Both asparagusate dehydrogenases catalyzed the reaction Asg(SH)2 + NAD+ equilibrium AsgS2 + NADH + H+ and exhibit lipoyl dehydrogenase and diaphorase activities. Lipoyl dehydrogenase is specific for lipoate and has no asparagusate dehydrogenase activity. NADP cannot replace NAD in any case. Optimum pH for substrate reduction of the three enzymes are near 5.9. Asparagusate dehydrogenases I and II have Km values of 21.5 mM and 20.0 mM for asparagusate and 3.0 mM and 3.3 mM for lipoate, respectively. Lipoyl dehydrogenase activity of asparagusate dehydrogenases is enhanced by NAD and surfactants such as lecithin and Tween 80, but asparagusate dehydrogenase activity is not enhanced. Asparagusate dehydrogenases are strongly inhibited by mercuric ion, p-chloromercuribenzoic acid, and N-ethylmaleimide. Amino acid composition of the three enzymes is presented and discussed.
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PMID:Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Physical, chemical, and enzymatic properties. 18 3

Millimolar concentrations of tervalent manganese pyrophosphate can partially activate nitrate reductase which has been inactivated with NADH and HCN. The tervalent manganese complex is nevertheless not reduced by NADH in the presence of the enzyme, that is, it is not a substrate for the diaphorase moiety of the nitrate reductase. Ferric o-phenanthroline, on the other hand, is a good diaphorase substrate, but fails to activate the inactive enzyme.
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PMID:Nitrate reductase from Chlorella vulgaris. Reaction with manganese (III) pyrophosphate and with ferric o-phenanthroline. 18 Dec 48

The protective action of aspartic acid on isolated and perfused rat liver was studied. In case of D-galactosamine intoxication the GOT, GPT and SDH activity and the lactate and pyruvate concentration in the perfusion medium were less augmented and the glycogen level in hepatic tissue was less diminished in animals treated with aspartic acid, as compared to controls. The histochemical applied (PAS reaction for glycogen, nucleic acids, NADH2-diaphorase, glucose-6-phosphatase and membrane-ATP-ase), also stated a protecting effect in the treated animals. The protective action of aspartate is hypothetically considered to be exerted by its capacity to reestablish the cellular deficit of pyridine nucleotides and thus to improve the synthesis of nucleic acids, glycoprotein and glycolipids or/and by its participation in various metabolic pathways.
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PMID:Protecting action of aspartate on the hepatic changes induced by D-galactosamine. 18 87


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