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:1.6.99.3 (diaphorase)
5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A sensitive enzyme immunoassay was developed for human angiotensin converting enzyme. Monoclonal antibodies specific for two unique converting enzyme epitopes were utilized to develop a two-site sandwich enzyme immunoassay. Alkaline phosphatase conjugated to the detecting antibody hydrolyzes nicotinamide adenine dinucleotide phosphate (NADP) to NAD. Subsequently, NAD is cycled between its reduced and oxidized forms by an alcohol dehydrogenase/diaphorase catalyzed redox cycle. Each cycle converts iodonitrotetrazolium violet to a highly colored formazan which is quantitated. With this assay, as little as 94 pg/ml of native converting enzyme is detectable without interference from either therapeutic or endogenous converting enzyme inhibitors.
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PMID:A sensitive two-site sandwich enzyme immunoassay for human angiotensin converting enzyme utilizing monoclonal antibodies. 169 77

Amperometric determination of nicotinamide adenine dinucleotide (reduced form) (NADH) at an immobilized-diaphorase (Dp) electrode is described. The measurement was conducted using ferrocenylmethanol as a mediator in a stirred solution at 0.20 V versus a saturated calomel electrode. A linear relationship between the steady-state current and the concentration of NADH was found over the range 0.005-0.125 mmol dm-3. The immobilized-Dp electrode showed outstanding stability and the current response reached a steady state within 2-3 seconds upon addition of NADH. The proposed electrode was used to follow the reactions of pig heart lactate dehydrogenase and horse liver alcohol dehydrogenase. The kinetic investigation using the immobilized-Dp electrode gave the kinetic parameters (Michaelis constants, Km values, and maximum velocities, Vm values), which were in satisfactory agreement with those determined by a conventional spectrophotometric method.
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PMID:Immobilized-enzyme electrode for nicotinamide adenine dinucleotide (reduced form) (NADH) sensing and application to the kinetic studies of NADH dependent dehydrogenases. 178 60

The control exerted in vivo by mitochondrial functions on the dynamics of glycolysis was investigated in starved yeast cells that were metabolizing glucose semianaerobically. Glycolytic oscillations were triggered after a pulse of glucose by inhibition of mitochondrial respiration with KCN, myxothiazol and antimycin A or in mutants in the bc1 complex (ubiquinol:cytochrome c reductase) that were largely deficient in respiratory capacity. Inhibition of the adenine nucleotide translocator by preincubation with bongkrekic acid also triggered a train of damped sinusoidal oscillations after glucose addition. The oscillations consisted of cycles of reduction and oxidation of the intracellular pool of nicotinamide nucleotides with periods of 45 s to 1 min and amplitudes of 0.8 mM or lower. Preincubation with the uncoupler carbonyl cyamide p-(trifluoromethoxy)phenylhydrazone (FCCP) annihilated cyanide-induced oscillations of NAD(P)H. Evidence for de-energization of mitochondrial membranes in vivo was obtained by mitochondrial staining with dimethylaminostyryl-methyl-pyridiniumiodine (DASPMI) of starved cells. The low rates of NADH reoxidation shown by respiratory mutants and the FCCP-treated X2180 strain open up the possibility that mitochondrial dehydrogenases also control glycolytic oscillations. Low rates of cytosolic NADH reoxidation induced by pyrazole, an inhibitor of alcohol dehydrogenase, were also associated with the disappearance of glycolytic oscillations. From experimental evidence and model calculations we conclude that the modulation of the levels of cytosolic ATP by mitochondrial functions in turn modulates the approach of the dynamic behavior of glycolysis to an oscillatory domain. The mitochondrial NADH dehydrogenase and the glycolytic steps associated with NADH reoxidation downstream from pyruvate appear to provide another control level of glycolysis dynamics in vivo.
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PMID:Dynamic regulation of yeast glycolytic oscillations by mitochondrial functions. 188 73

The NADPH-cytochrome P450 reductase gene isolated from the yeast Saccharomyces cerevisiae [Yabusaki et al., J. Biochem. 103, 1004-1010 (1988)] was expressed on a multi-copy plasmid in the yeast. The transformed yeast cells with the recombinant plasmid carrying the reductase gene with a length of 3 kb produced the corresponding mRNA read from the original transcription initiation site under the control of its own promoter with a maximum length of 300 bp. The reductase content in the transformed cells was 25 times higher than that of the endogenous reductase. When the coding region for the reductase was placed between the alcohol dehydrogenase I gene promoter and the terminator of the expression vector pAAH5, the expression level was 32 times higher than at the endogenous level. These recombinant yeast strains showed enhanced cytochrome c reductase activity with increased cellular reductase levels. A simultaneous expression of yeast P450 reductase with rat P450c or bovine P450(17 alpha) resulted in 25 times or a 5 times increase in the corresponding P450-dependent monooxygenase activity of the recombinant yeast strains, respectively, as compared with that of the yeast cells expressing the corresponding P450 species. These results suggested that the overproduction of yeast P450 reductase with a simultaneous expression of the mammalian P450 species enhanced the P450c- and P450(17 alpha)-dependent monooxygenase activities in the recombinant yeast strains, probably due to the increased frequency of the interaction between yeast P450 reductase and P450c or P450(17 alpha) in the yeast microsomes.
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PMID:Expression of cloned yeast NADPH-cytochrome P450 reductase gene in Saccharomyces cerevisiae. 212 33

On the material of early autopsies of the above patients the activity of the following myocardial enzymes was undergone the quantitative histochemical study: succinate, lactate, (beta-oxybutyrate, d-glycerophosphate, glucose 6-phosphate and alcohol dehydrogenase, NAD-diaphorase, catalase, phosphorylase. The increase of the activity of practically all enzymes studied was observed in the myocardial areas with no circulation disturbances. This increase was due to the moderate myocardial hypertrophy. On the contrary, in the areas with a non-even blood supply (ischemia) the decrease of the activity of all oxidative-reductive enzymes was observed. The presence of such foci in the myocardium which occur in 70% cases studied facilitates the development of the ventricular fibrillation with a fatal outcome. The enzyme depression is particularly pronounced against the background of a high alcoholic content.
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PMID:[A histochemical study of enzyme activity in the myocardium of victims of sudden death with small-focal cardiosclerosis]. 259 77

The effect of the glucose analogue 5-thio-D-glucose (5TG) on the yeast Saccharomyces cerevisiae was studied. Derepression of mitochondrial respiratory chain cytochromes, alcohol dehydrogenase (isoenzyme II), NADH dehydrogenase and maltase was inhibited by 0.5-2 mM-5TG. Growth rate was only slightly affected. Ethanol was efficiently produced with 2 mM-5TG in medium initially containing 0.25% glucose. Mutants resistant to the growth inhibitory effects of 5TG on glycerol medium showed resistance to the catabolite repressing effects of glucose. Other mutants, known to be catabolite repression resistant, showed resistance to 5TG. The analogue seems to inhibit derepression of glucose repressible enzymes with greater potency than glucose itself.
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PMID:Catabolite repressive effects of 5-thio-D-glucose on Saccharomyces cerevisiae. 330 35

The genetic control of NADH dehydrogenase-1 (NDH-1) and aromatic alcohol dehydrogenase-2 (AADH-2) was investigated in Triticum aestivum cv. Chinese Spring. Evidence was obtained that NDH-1 is active as a monomer and is encoded by genes located in the p arms of the homoeologous group 4 chromosomes. The NDH-1 gene loci located in 4Ap, 4Bp, and 4Dp were designated Ndh-A1, Ndh-B1, and Ndh-D1, respectively. Aadh-A2 was previously reported to be located in 6Aq; in this study, Aadh-B2 and Aadh-D2 were localized in 6Bq and 6Dq, respectively. Alcohol dehydrogenase-1 is expressed on AADH-2 zymograms; the presence of a contaminating aliphatic alcohol in one or more reagents is suggested as the probable cause of this phenomenon.
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PMID:Genetic control of NADH dehydrogenase-1 and aromatic alcohol dehydrogenase-2 in hexaploid wheat. 332 6

A method is described for increasing the response of enzyme immunoassays employing alkaline phosphatase as the label initiating 2 sequential catalytic reactions. First, NADP is dephosphorylated to produce NAD, which catalytically activates a specific redox-cycle involving the enzymes alcohol dehydrogenase and diaphorase. During each turn of the cycle 1 molecule of a tetrazolium salt is reduced to an intensely coloured formazan. The method is capable of detecting as little as 0.01 amol alkaline phosphatase, and when applied to an immunoassay for TSH a sensitivity (zero + 2.5 standard deviations) of 0.0013 mIU/l was obtained.
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PMID:Enzyme amplification for immunoassays. Detection limit of one hundredth of an attomole. 351 23

Study of the activity of some myocardial enzymes in sudden death cases with alcoholic cardiomyopathy (ACMP) was made by quantitative histochemical methods. The decrease of dehydrogenase activity of succinate, lactate, beta-hydroxybutyrate, alpha-glycerophosphate and NAD-diaphorase was found in line with the increase of the activity of glucose-6-phosphate dehydrogenase, alcohol dehydrogenase and catalase versus control (myocardium of those who died of trauma). Disorders of major metabolic processes in the myocardium may occasionally lead to electrical instability resulting in ventricular fibrillation and sudden cardiac death. In almost 80% of sudden cardiac deaths in ACMP foci of acute myocardial ischemia are found, that can lead to ventricular fibrillation with lethal outcome.
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PMID:[Histoenzymologic characteristics of the myocardium in sudden death in patients with alcoholic cardiomyopathy]. 380 Jun 78

Zinc content of testes, bones, esophagus, kidneys, and muscles was decreased, whereas iron content was increased in the testes of zinc-deficient rats compared to restrictedly fed control rats. Histochemical enzyme determinations revealed reduced activities of certain enzymes in the testes, bones, esophagus, and kidneys. In the testes, lactic dehydrogenase (LDH), malic dehydrogenase (MDH), alcohol dehydrogenase (ADH), and NADH diaphorase; in the bones, LDH, MDH, ADH, and alkaline phosphatase; in the esophagus, MDH, ADH, and NADH diaphorase; and in the kidneys, MDH and alkaline phosphatase were decreased in zinc-deficient rats compared to restrictedly fed controls. Succinic dehydrogenase (SDH) revealed no significant changes under the conditions of our experiments in various groups of rats that were investigated. In a "repleted" group of rats, content of zinc in testes and bones increased significantly, compared to the deficient group. The iron content of the testes decreased after repletion with zinc. In the testes, bones, esophagus, and kidneys, the activities of various enzymes increased after repletion with zinc. Inasmuch as the major manifestations of zinc deficiency syndrome in the rat include growth retardation, testicular atrophy, and esophageal parakeratosis, our results suggest that the content of zinc in the above tissues most likely controls the physiological processes through the formation of zinc-dependent enzymes.
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PMID:Studies on zinc deficiency: changes in trace elements and enzyme activities in tissues of zinc-deficient rats. 429 21


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