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)

Experiments were conducted on rabbits. A study was made of the activity of the redox enzymes--glucose-6-phosphate dehydrogenase (G-6-PDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NAD-and NADP-diaphorases, cytochromeoxidase (CCO), alpha-glycerophosphate dehydrogenase (alpha-GPDH) in the supraoptic and paraventricular nuclei of the hypothalamus and the posterior lobe of the hypophysis under conditions of stimulation and removal of the superior cervical sympathetic ganglia. There was revealed a correlation between the activity of the tissue respiration enzymes (SDH, MDH, NAD- and NADP-diaphorase, CCO) and the functional condition of the hypothalamo-neurohypophysial neurosecretory system. However, the enzymes of the pentose-phosphate (G-6-PDH) and glycerophosphate shunt (alpha-GPDH) and also of the anaerobic way of oxidation (LDH) reacted nonspecifically on the induced effects.
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PMID:[Effect of removal and stimulation of the superior cervical sympathetic ganglia on the activity of oxidation-reduction enzymes in the neurosecretory cells of the anterior hypothalamus in rabbits]. 20 40

Three pyridine nucleotide-dependent diaphorases have been isolated from Acinetobacter calcoaceticus cells and partially characterized. Two of them, with molecular weights of 165,000 and 57,000, utilize NADPH as electron donor whereas the third one (MW = 57,000) is specific for NADH. Oxidized viologen dyes, flavin nucleotides, dichlorophenol indophenol and ferricyanide can act with efficiency as acceptors in the reaction mediated by these diaphorases. The diaphorase activities have been characterized kinetically, and the effect of different inhibitors and cofactors has been also studied. The diaphorases seem to be subjected to metabolic control by oxidation and reduction.
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PMID:NADH and NADPH-viologen reductases from Acinetobacter calcoaceticus. 22 3

The distribution of simian virus 40 large tumor antigen in subcellular fractions from simian virus 40-transformed hamster (H-50) and mouse (VLM) cells and from simian virus 40-infected monkey cells was determined. Solubilized [(35)S]-methionine- or (32)P(i)-labeled surface membrane and nuclear fractions were prepared, immunoprecipitated with hamster anti-T serum, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Tumor antigen with an apparent molecular weight of approximately 96,000 was detected in both subcellular fractions. Minor components of approximately 68,000 and approximately 56,000 with anti-T reactivity which labeled with [(35)S]methionine were also detected in both fractions from H-50 cells, as were components of approximately 140,000 and approximately 56,000 from VLM cells. The 56,000 component appeared to be greatly reduced in (32)P(i)-labeled surface membrane fractions. Normal cells or cells transformed with a heterologous agent, such as polyoma virus or a chemical carcinogen, lacked immunoprecipitable tumor antigen. Cell fractionation was monitored by [(3)H]thymidine labeling, NADH-diaphorase activity, and Na(+)-K(+)-dependent ATPase activity. These analyses revealed only trace contamination of surface membranes by nuclei, extremely low levels of nuclear rupture during homogenization, and an approximate 10-fold enrichment of surface membrane. Reconstruction experiments demonstrated that soluble tumor antigen failed to associate or copurify with surface membranes during fractionation procedures. These results indicate the presence of a protein in the plasma membrane of cells transformed or infected by simian virus 40 that is immunologically indistinguishable from nuclear tumor antigen.
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PMID:Subcellular Localization of simian virus 40 large tumor antigen. 22 15

Paraquat mediates a superoxide dismutase-inhibitable reduction of cytochrome c by suspensions of Escherichia coli B. Glucose was most effective in providing electrons for this cytochrome c reduction, but other nutrients could serve in this capacity, provided the cells were preconditioned by growth on these nutrients. Paraquat reduction depended upon a NADPH:paraquat diaphorase, present in the cytosol. Reduced paraquat could diffuse across the cell envelope and react with dioxygen, in the suspending medium, thus generating O2- in that compartment. Most of the paraquat reduced in the cell, under the conditions used, reoxidized in situ and most of the O2- production was thus intracellular. The partitioning of reduced paraquat between intracellular and extracellular compartments, prior to reaction with dioxygen, depended upon intracellular pO2 and any strategy which raised intracellular pO2 decreased the efflux of reduced paraquat and thus decreased extracellular O2- production. Extracellular O2- and H2O2 did contribute to cell damage in proportion to the amount produced. O2- appeared to be unable to cross the cell envelope in either direction and the only O2- which was effective in raising the rate of biosynthesis of the manganese-superoxide dismutase, was that generated within the cell.
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PMID:Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. 22 55

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
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PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

The Co- and Ru-substituted derivatives of adrenal iron-sulfur protein (adrenodoxin) were prepared from its apoprotein in the presence of urea, dithiothreitol, Na2S, and metal ions. Both metal-substituted proteins had 2 g-atoms each of metal and labile sulfur per mole of protein. The Co derivative had optical absorption maxima at 257, 264, 470, and 1430 nm with shoulders at 275, 280, 300, and 380 nm. The molar extinction coefficient per Co atom was 2.200 M-1 cm-1 at 470 nm. The Ru derivative had a broad maximum at 500 nm with a molar extinction coefficient of approximately 100 M-1 cm-1 per Ru atom. The visible chromophore of the Co- and Ru-substituted proteins with mercurials revealed that the saturation levels are 8.6 and 8.4 mol of mercurial/mol of protein. The values agree with that of the native protein within experimental errors. The tyrosyl residue at position 82 displayed a broad anomalous emission at 335 and 331 nm for the Co- and Ru-substituted proteins, respectively, as well as in the case of the native protein. There was no electron paramagnetic resonance signal of the Co derivative in a wide magnetic field at 77 degrees K. Additionally, the Co and Ru derivatives had no enzymatic activity toward NADPH-cytochrome c reduction in the presence of adrenal diaphorase (adrenodoxin reductase). There was no indication that Mn, Ni, Cu, and Os are incorporated into the apoprotein in the presence of urea. Incorporation of Fe into the protein was examined in the presence of Co or Ru. In a system containing both Fe and Ru, Fe was exclusively incorporated into the protein. In contrast to this, the reaction products from a system containing both Fe and Co were found to consist of both Fe and Co derivatives at approximately equimolar quantity.
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PMID:Cobalt and ruthenium replacement for iron in adrenal iron-sulfur protein (adrenodoxin). Preparation and some properties. 23 19

A dihydrodipicolinate reductase containing flavin was purified from sporulating Bacillus subtilis PCI 219. The purified enzyme appeared homogeneous by dise gel electrophoresis. Its molecular weight was estimated as 74,000 by gel filtration on Sephadex G-200, and as 18,500 by electrophoresis on sodium dodecylsulfate polyacrylamid gel. These results suggest that the enzyme is composed of four subunits. The prosthetic group was identified as FMN, and one mole of the enzyme contained two moles of FMN. Both NADPH and NADH acted as coenzyme, though NADH was less effective. The enzyme also exhibited diaphorase activity. The pH optimum was 6.1. The enzyme was inhibited by dipicolinate but not by lysine or alpha, epsilon-diaminopimelate.
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PMID:A new flavin enzyme catalyzing the reduction of dihydrodipicolinate in sporulating Bacillus subtilis I. Purification and properties. 23 91

The use of cinnamyl nitroblue tetrazolium chloride (DS-NBT) in dehydrogenase experiments (lactic dehydrogenase, succinic dehydrogenase, nicotinamide adenine dinucleotide diaphorase) and 3,3'-diaminobenzidine tetrahydrochloride (DAB) in cytochrome oxidase experiments indicated that mitochondrial oxidoreduction reactions from nicotinamide adenine dinucleotide to cytochrome oxidase are located on the inner mitochondrial membrane in the outer compartment and the intracristate spaces. These reactions behave according to the chemiosmotic hypothesis. The cochlear hair cell mitochondria are cytochemically indistinguishable from free liver mitochondria. The heterogeneous mitochondrial staining pattern is related to the osmolarity of the incubation media, solubility of the enzymes and pH of the medium, but not to the fixation method.
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PMID:The ultrastructural cytochemistry of lactic dehydrogenase, succinic dehydrogenase, dihydro-nicotinamide adenine dinucleotide diaphorase and cytochrome oxidase activities in hair cell mitochondria of the guinea pig cochlea. 23 41

The activity of some enzymes in T- and B-lymphocytes from the spleen of CBA mice was investigated. T-cell suspension was obtained by using a modified Kedar et al. method based on immunosorption. EAC-rosette forming cells were studied in the capacity of B-cells. The activity of all the enzymes examined proved to be higher in T-lymphocytes than in B lymphocytes; the greatest difference was noted in the activity of NADP.H2-diaphorase, and the least--in the activity of NAD.H2-diaphorase.
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PMID:[Activity of a number of enzymes in the splenic T- and B-lymphocytes of CBA strain mice]. 31 70

1. Like the malate dehydrogenases of eucaryotic cells, the Propionibacterium shermanii enzyme is a dimer consisting of two 35,000 molecular weight subunits. 2. In electrophoretic behavior, resistance to substrate inhibition and stability to heating and dilution the P. shermanii MDH is more similar to the s-MDH than to the m-MDH of pig heart. 3. The P. shermanii MDH has a high turnover number (ca. 140,000) as well as Km values for both L-malate and oxalacetate which are four times higher than the mammalian isoenzymes. 4. A coupled assay for MDH using the malate-lactate transhydrogenase and diaphorase is described in which both substrates, L-malate and NAD, are regenerated.
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PMID:A comparison of the malate dehydrogenase of the propionic acid bacteria with the mammalian soluble and mitochondrial isoenzymes. 31 44


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