Results 261 to 270 of about 623,822 (311)
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Glutathione reductase functions as vanadate(V) reductase
Archives of Biochemistry and Biophysics, 1990The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to
X L, Shi, N S, Dalal
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Journal of Neurochemistry, 1980
AbstractHuman brain contains multiple forms of aldehyde‐reducing enzymes. One major form (AR3), as previously shown, has properties that indicate its identity with NADPH‐dependent aldehyde reductase isolated from brain and other organs of various species; i.e., low molecular weight, use of NADPH as the preferred cofactor, and sensitivity to inhibition ...
P L, Hoffman +2 more
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AbstractHuman brain contains multiple forms of aldehyde‐reducing enzymes. One major form (AR3), as previously shown, has properties that indicate its identity with NADPH‐dependent aldehyde reductase isolated from brain and other organs of various species; i.e., low molecular weight, use of NADPH as the preferred cofactor, and sensitivity to inhibition ...
P L, Hoffman +2 more
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Current Drug Metabolism, 2010
Enzymatic carbonyl reduction means the formation of a hydroxy function out of a ketone or aldehyde moiety and applies for the metabolism of physiological (endogenous) or xenobiotic (exogenous) molecules. As for endogenous substrates, carbonyl reduction is often part of a reversible oxidoreductase process and involves the activation or inactivation of ...
Petra, Malátková +2 more
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Enzymatic carbonyl reduction means the formation of a hydroxy function out of a ketone or aldehyde moiety and applies for the metabolism of physiological (endogenous) or xenobiotic (exogenous) molecules. As for endogenous substrates, carbonyl reduction is often part of a reversible oxidoreductase process and involves the activation or inactivation of ...
Petra, Malátková +2 more
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Pharmacotherapy: The Journal of Human Pharmacology and Drug Therapy, 1990
The present management of diabetes consists of attempting to control blood sugar tightly in the normal range and to treat individual complications such as neuropathy and retinopathy as they appear. Whereas these measures are perhaps effective in slowing the progress of diabetic complications, they do not cure the underlying process.
W R, Kirchain, M S, Rendell
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The present management of diabetes consists of attempting to control blood sugar tightly in the normal range and to treat individual complications such as neuropathy and retinopathy as they appear. Whereas these measures are perhaps effective in slowing the progress of diabetic complications, they do not cure the underlying process.
W R, Kirchain, M S, Rendell
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Nature, 1958
THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
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THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
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Dihydromorphinone ketone reductases
Life Sciences, 1975Abstract Dihydromorphinone ketone reductases are new NADPH dependent drug metabolizing enzymes which occur predominantly in cytosol of liver and to a lesser extent in kidney and lung. The hepatic enzyme of the chicken has been found to differ from that of rabbit with respect to relative effectiveness of inhibitors and according to certain other ...
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Current Opinion in Chemical Biology, 2004
The ability of some anaerobic bacteria to conserve energy via a soluble substrate level phosphorylation system by reducing glycine to acetyl-phosphate has been an intriguing mechanism for about half a century. The genes implicated in this system have been sequenced and form an operon structure with those of the thioredoxin system.
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The ability of some anaerobic bacteria to conserve energy via a soluble substrate level phosphorylation system by reducing glycine to acetyl-phosphate has been an intriguing mechanism for about half a century. The genes implicated in this system have been sequenced and form an operon structure with those of the thioredoxin system.
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NADH-Ferric Reductase Activity Associated with Dihydropteridine Reductase
Biochemical and Biophysical Research Communications, 2000In mammals dietary ferric iron is reduced to ferrous iron for more efficient absorption by the intestine. Analysis of a pig duodenal membrane fraction revealed two NADH-dependent ferric reductase activities, one associated with a b-type cytochrome and the other not.
P L, Lee +3 more
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Inhibition of aldehyde reductase by aldose reductase inhibitors
Biochemical Pharmacology, 1990A broad group of structurally diverse aldose reductase inhibitors including flavonoids, carboxylic acids and hydantoins, have been examined for their ability to inhibit rat kidney aldehyde reductase (EC 1.1.1.19, EC 1.1.1.20) versus rat lens aldose reductase (EC 1.1.1.21).
S, Sato, P F, Kador
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Journal of Neurochemistry, 1985
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
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Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
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