Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Aromatic ketone reductase activity of microsomes showed a unique cofactor requirement: Addition of NADP and glucose-6-phosphate was as effective as that of an artificial NADPH generating system, whereas NADPH alone served as a cofactor less efficiently. Microsomal aromatic ketone reductase, purified partially from guinea pig liver microsomes after solubilization with Triton X-100, reduced 5 beta-dihydrotestosterone, aromatic aldehydes, and ketones with NADPH as a cofactor. However, addition of hexose-6-phosphate dehydrogenase, purified from the same source, as an NADPH generator produced about 2 times higher activity than that of yeast glucose-6-phosphate dehydrogenase or NADPH alone.
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PMID:A possible functional relationship between microsomal aromatic aldehyde-ketone reductase and hexose-6-phosphate dehydrogenase. 699 53

An NADPH-specific aromatic aldehyde-ketone reductase located in guinea pig liver microsomes can be effectively solubilized with nonionic detergents, but not with bile salts and hydrolytic enzymes. Destruction of microsomal membranes by nonionic detergents or acetone treatment leads to significant activation of the reductase, indicating that the enzyme is partly latent in intact microsomes. After solubilization with Triton X-100, the reductase has been highly purified. The purified enzyme catalyzes the NADPH-linked reduction of xenobiotic aromatic aldehydes and ketones as well as 3-ketosteroids, notably 5 alpha- and 5 beta-dihydrotestosterones. The reductase activities for xenobiotic carbonyl compounds and for 3-ketosteroids are each inhibited by addition of the other type of substrate and show the same pH optimum, cofactor requirement, and heat stability, indicating the same enzyme is responsible for the reduction of the two types of substrates. Hexose-6-phosphate dehydrogenase, purified from guinea pig liver microsomes, acts as a more effective NADPH generator for the reductase than yeast and guinea pig liver cytosolic glucose-6-phosphate dehydrogenase. Evidence has been obtained that hexose-6-phosphate dehydrogenase undergoes a functional interaction with the reductase, facilitating the provision of NADPH to the reductase activity both in the reconstituted system and in microsomes.
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PMID:Microsomal reductase for aromatic aldehydes and ketones in guinea pig liver. Purification, characterization, and functional relationship to hexose-6-phosphate dehydrogenase. 703 Oct 45

Human erythrocytes were separated into three groups according to their density and age by centrifugation in a continuous Percoll gradient. The specific activities of glucose-6-phosphate dehydrogenase, catalase, glutathione peroxidase, glutathione reductases as well as the glutathione and selenium content were highest in the youngest cell and uniformly decreased by about 20-30% in the eldest group. The age-dependence of superoxide dismutase was much more pronounced. The malondialdehyde content taken as an estimate for lipid peroxidation showed an inverse age dependence and increased by 35% in the eldest cell population. Red blood cells from 10 anemic patients exhibited less glutathione and also less malondialdehyde, while GSH-peroxidase and GSSG-reductase contents were higher. The parameters showed similar age profiles as in healthy subjects. The findings support the concept of lipid peroxidation as one of the causal events in red cell aging, but do not allow to deduce the involvement of a single enzyme related to the glutathione redox cycle in this process.
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PMID:[Activity of the glutathione redox system in human erythrocytes at various ages]. 713 38

The paper is concerned with the effect of epiphysisectomy on the glucose-6-phosphate dehydrogenase, glutathion reductase, succinate dehydrogenase activities and the content of sodium and potassium in the cortex and medullary layers of the kidneys under spontaneous diuresis and water load. It is shown that in rats without epiphysis the activity of glucose-6-phosphate dehydrogenase is lowered both in the cortex and medullary layers of the kidneys. The activity of glutathion reductase rises in the cortex layer of the kidneys only under water load. A disturbance is found in the sodium and potassium distribution between the cortex and medullary layers of the kidneys. An assumption is advanced on a possible role of epiphysis in regulating the kidney functions.
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PMID:[Glucose-6-phosphate dehydrogenase, glutathione reductase, succinate dehydrogenase activities and content of sodium and potassium in kidneys of epiphysisectomized rats under spontaneous diuresis and water load]. 725 56

Two new glucose-6-phosphate dehydrogenase (G6PD, D-glucose 6-phosphate: NADP oxido reductase, E.C. 1.1.1.49) variants, designated G6PD Napoli and G6PD Ferrara II, are described in propositi from two unrelated families. Characterization side by side of the two variants according to W.H.O. recommendations reveals minor differences which are mostly related to utilization of artificial substrates (increased in both cases as compared with normal G6PD type B). Other properties, which are not significantly distinctive between the two variants, are an enzyme activity amounting to nearly 20% of normal, a decreased electrophoretic mobility, decreased Km values for glucose-6-phosphate and NADP, normal thermostability and biphasic pH curves. However, marked differences emerged between the two variants and between either variant and G6PD B as well, when a number of microtechniques were used. These were: (1) the half-lives of G6PD Napoli and G6PD Ferrara II are 16 and 29 d, respectively, while that of G6PD B is 63 d; (2) the specific activities, measured by a method involving direct estimation of G6PD protein on sodium dodecyl sulphate polyacrylamide gel electrophoretic tracings, are 166 I.U./mg (G6PD Napoli) and 59 I.U./mg (G6PD Ferrara II), as compared with normal value of 180 I.U./mg (G6PD B). On the whole, these findings allow the conclusion that the deficiency of catalytic activity is related to an accelerated though distinctive decay of both mutant enzyme proteins within the affected erythrocytes and that a significant impairment of catalytic efficiency is also involved, as a result of the underlying structural mutation in the case of G6PD Ferrara II.
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PMID:G6PD Napoli and Ferrara II: two new glucose-6-phosphate dehydrogenase variants having similar characteristics but different intracellular lability and specific activity. 725 90

The relationship between D-glucose-6-phosphate: NADP oxido-reductase (E.C.1.1.1.49; glucose-6-phosphate dehydrogenase; G6PD) deficiency and homozygous sickle cell (SS) disease was examined in 120 patients. The proportions of hemizygotes (22.6%) was slightly more than that observed, and the combined proportions of heterozygotes and homozygotes (28.3%) were slightly less than would be expected, in the general population, but the differences were not significant. However, the proportion of patients of abnormal G6PD status in the 10-19 years age group was 41.7%, significantly more than that found in the 20-29 years age group (0.02 less than P less than 0.05), or expected in the general population (P=0.05). Possible reasons for this are discussed. Difference in G6PD status did not affect the total haemoglobin concentration, reticulocyte count, unconjugated serum bilirubin or Hb F concentration, irreversibly sickled cell counts or plasma haemoglobin concentration, and there was no demonstrable correlation between clinical severity or leg ulceration and abnormal G6PD status.
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PMID:Glucose-6-phosphate dehydrogenase deficiency and homozygous sickle cell disease in Jamaica. 737 31

Cyanosis in a 36 year old patient which persisted 20 years after a successful surgical closure of her patent foramen ovale has been finally diagnosed as due to congenital methemoglobinemia: a 28% level of methaemoglobin and no activity od NAD-dependent methaemoglobin reductase were found. Erythrocyte antioxidative system was studied i.e. glutathione peroxidase, reductase, transferase, superoxidase dismutase and glucose-6-phosphate dehydrogenase. Increased activity was disclosed of superoxide dismutase and glucose-6-phosphate dehydrogenase in erythrocytes in comparison to normal individuals as well as increased concentration of lipid peroxidation products coexisting with methaemoglobin reductase deficiency.
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PMID:[Congenital methemoglobinemia found in an adult. Case report]. 749 53

Treatment of rats with daily doses of 20 mg of lindane/kg for 3 consecutive days led to the accumulation of the insecticide in several tissues, including erythrocytes and liver. Lindane did not alter the hematocrit and hemoglobin concentration but reduced methemoglobin levels by 17%. Red blood cells from controls and lindane-treated rats, exposed to t-butyl hydroperoxide, exhibited comparable rates of oxygen uptake and visible chemiluminescence, whereas the induction period that precedes oxygen uptake was significantly enhanced in the latter group. Lindane treatment did not modify the activity of erythrocyte glutathione peroxidase, glucose-6-phosphate dehydrogenase, catalase, and methemoglobin reductase, being the total content of glutathione and superoxide dismutase activity significantly increased. The liver from lindane-treated rats showed an enhanced microsomal pro-oxidant activity, evidenced by higher cytochrome P450 content and NADPH-cytochrome c reductase and NADPH oxidase activities. The higher enzyme activities led to an increased superoxide anion generation (adrenochrome formation) and lipid peroxidation (measured either by the production of thiobarbituric acid reactants and spontaneous visible chemiluminescence). Concomitantly, liver glutathione content and the activity of glutathione peroxidase-glutathione reductase couple were augmented by lindane treatment, without any change in superoxide dismutase activity, together with a reduction in that of catalase. Results suggest that lindane does not alter the prooxidant/antioxidant status of the erythrocyte in conditions of a significant cellular accumulation of the insecticide, which might exert direct action on enzymatic systems leading to enhanced superoxide dismutase activity and glutathione content.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Acute lindane intoxication: a study on lindane tissue concentration and oxidative stress-related parameters in liver and erythrocytes. 751 43

The effects of a low fat diet or diets enriched with either n-6 or n-3 polyunsaturated fatty acids (safflower or fish oil, respectively) on lipid metabolism in periportal and pericentral zones of female rat liver lobules were investigated in relation with cell proliferation after partial hepatectomy. It was found that cell proliferation was localized almost exclusively in periportal and midzonal areas and was significantly reduced by 60% after a fish oil diet only. The fish oil diet caused a strongly increased beta-oxidation capacity in peroxisomes and a moderately increased catalase activity. Catalase activity was mainly localized pericentrally, particularly after partial hepatectomy, whereas the capacity of lipid peroxidation product formation was doubled only in periportal zones in rats on a fish oil diet. The capacity of glucose-6-phosphate dehydrogenase activity to produce NADPH was distinctly lower in both zones of liver lobules as a result of the fish oil diet. Localization patterns and activity in liver lobules of NADPH-cytochrome c (P450) reductase were not significantly affected by fish oil diet. Therefore, it is concluded that elevated peroxisomal beta-oxidation and increased lipid peroxidation capacity in periportal zones of liver lobules coincide with reduced cell proliferation in hepatectomized rats on fish oil diet. These findings support the hypothesis that lipid peroxidation products are involved in the regulation of cell proliferation.
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PMID:Effects of n-3 and n-6 polyunsaturated fatty acid-enriched diets on lipid metabolism in periportal and pericentral compartments of female rat liver lobules and the consequences for cell proliferation after partial hepatectomy. 759 92

More than 1500 umbilical blood samples from newborns were examined by modified analytical isoelectric focussing method on polyacrylamide-ampholine gels at Ph3.5-9.5 and 5.5-8.5 with Multiphor-2117. Hemoglobin fractions were measured by laser densitometer 22P2 (LKB, Sweden). Methemoglobinemia type was identified by methemoglobin content, methemoglobin reductase activity, Betke's coefficient, and by analyzing the spectra of blood hemolysates containing group M hemoglobin. Methemoglobinemia due to low methemoglobin reductase activity was detected in one child. Increased levels of methemoglobin were detected in his father, mother, grandmother, and grandfather. Methemoglobin reductase activity was not detected in the proband, his mother and grandfather. Zero methemoglobin reductase activity in the proband was combined with zero glucose-6-phosphate dehydrogenase activity. Grandmother was found to be a heterozygotic carrier of these enzymes genes. Glutathione reductase activity was found reduced below the norm in all the members of this family.
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PMID:[Familial case of methemoglobinemia associated with glucose-4-phosphate dehydrogenase deficiency]. 775 71


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