Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT00568 (ascorbate)
 23,072 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using spin stabilization, ESR measurements have been made of o-semiquinone production from the horseradish peroxidase-H2O2 oxidation of catecholamine substrates. The termination rate constant for semiquinones stabilized with Zn2+ at pH 5 is about 10(4) times smaller than for uncomplexed semiquinones at neutral pH. Stabilization allows steady state concentrations of semiquinones to be obtained. The duration of the steady state is dependent upon the concentrations of enzyme, hydrogen peroxide, and catecholamine substrate. The relative reactivity of the substrates 3,4-dihydroxyphenylalanine, norepinephrine, and dopamine at pH 5 is 1:8:40. The effects of phenol and ascorbate were studied and shown to be consistent with scavenging of phenoxyl radicals by catecholamine and semiquinone radicals by ascorbate, respectively.
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PMID:Peroxidatic oxidation of catecholamines. A kinetic electron spin resonance investigation using the spin stabilization approach. 633 64

The neutral alpha-tocopheroxyl radicals, generated in monolayers on silica gel containing alpha-tocopherol and partly autoxidised methyl linoleate at 90 degrees C, were detected and identified by ESR spectroscopy. Addition of ascorbic acid to the monolayer resulted in the complete quenching of the alpha-tocopheroxyl radical spectrum. This lends support to the view that ascorbate transfers hydrogen to alpha-tocopheroxyl radicals thus regenerating alpha-tocopherol.
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PMID:Electron spin resonance study of the role of vitamin E and vitamin C in the inhibition of fatty acid oxidation in a model membrane. 662 32

The rate of free radical formation in aqueous solutions of ascorbic acid in the presence of chelating agents was measured by the ESR-stopped-flow method. Addition of ethylenediamine tetraacetate and trimetaphosphoric acid to the ascorbic acid-oxygen system results in only a minimal change in the rate of ascorbate free radical formation compared to that in absence of inhibitors. Evidence suggests that radical formation arises via secondary reactions involving products.
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PMID:The effect of inhibitors on the radical formation in aqueous solutions of ascorbic acid. 680 4

The concentrations of total ascorbic acid, reduced and oxidized forms of ascorbic acid, the ESR intensity of ascorbate radical, and the ratio of oxidized form of ascorbic acid to total ascorbic acid (DAsA/AsA) were estimated on 217 healthy controls, whose ages ranged from 12 to 96 years, in order to examine influences of sex and age. The concentration of total ascorbic acid was higher in females than in males throughout all age classes, but the oxidized form did not show a sex difference. Then it was found that the reduced form was higher in females than in males throughout all age classes. The concentrations of total ascorbic acid and reduced and oxidized forms of ascorbic acid, and the ESR intensity declined with age, but the DAsA/AsA ratio increased with age.
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PMID:Influences of sex and age on serum ascorbic acid. 686 81

In the present work, we studied the effects of phenoxyl radicals, generated by tyrosinase-catalyzed oxidation of a phenolic antitumor drug, Etoposide (VP-16), on a purified dog kidney Na+/K(+)-ATPase by characterizing interactions of VP-16 phenoxyl radicals with the enzyme's SH-groups by ESR and correlating the loss of the enzymatic activity with the oxidation of its SH-groups, and oxidation of VP-16. VP-16/tyrosinase caused inhibition of Na+/K(+)-ATPase which was dependent on the incubation time and concentration of tyrosinase. The inhibition of Na+/K(+)-ATPase was accompanied by a decrease of DTNB (5,5'-dithiobis-(2-nitrobenzoic acid)-titratable SH-groups. In the presence of Na+/K(+)-ATPase, a typical ESR signal of the VP-16 phenoxyl radical could be observed only following a lag period the duration of which was proportional to the concentration of the Na+/K(+)-ATPase added. Our HPLC measurements demonstrated that Na+/K(+)-ATPase protected VP-16 against tyrosinase-catalyzed oxidation. Combined these results suggest that redox-cycling of VP-16/VP-16 phenoxyl radical by SH-groups of Na+/K(+)-ATPase occurred. Ascorbate which is known to reduce the VP-16 phenoxyl radicals, protected the enzyme against inactivation, prevented oxidation of the enzyme's SH-groups. Reduction of VP-16 phenoxyl radicals by ascorbate was directly observed by the semidehydroascorbyl radical signal in the ESR spectra. VP-16 phenoxyl radical-induced oxidation of sulfhydryls and inhibition of the Na+/K(+)-ATPase may be responsible for at least some of its clinical side effects (e.g., cardiotoxicity) which can be prevented by ascorbate.
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PMID:Inhibition of Na+/K(+)-ATPase by phenoxyl radicals of etoposide (VP-16): role of sulfhydryls oxidation. 749 37

We measured Asc.- (ascorbate radical) produced by the reaction of AscH- (ascorbic acid) with HO. or O2.- after irradiation in mouse. It is possible to measure Asc.- easily using ESR and a dialysis method in which Asc.- was collected at room temperature in the interstitial fluid through the dialysis membrane. After irradiation, Asc.- increased in both normal muscle and tumour tissues (SCC-VII) in proportion to the radiation dose. Asc.- increased after treatment with the agents H2O2 and FeCl2, while it decreased after treatment with SOD and catalase. These results suggest that the amount of HO. and O2.- produced is reflected in the Asc.- production. Also, the increase in Asc.- production when WR-2721 was administered prior to irradiation was less than for experiments in which irradiation only was performed. This method is useful for the following reasons. First, no special treatment, such as freezing of the sample, and no administration of noxious agents are necessary to measure Asc.-. Second, irradiation using a dose of only a few Gy shows an increase in production of Asc.-. Third, this method does not require removal of organs. Using this method, Asc.- can serve as an indicator of the amount of HO. and O2.- produced by irradiation in vivo.
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PMID:Detection of an increase in ascorbate radical in an irradiated experimental tumour system using ESR. 759 73

Exposure of cupro-zinc superoxide dismutase (SOD) to hydrogen peroxide or ascorbate-Fe(III) gives rise to the extensively oxidative modification of SOD. The results showed as (1) the enzyme was irreversibly inactivated by H2O2 and ascorbate-Fe(III); (2) both human and bovine SOD showed an increase in reactivities with their antibodies; (3) the reduction and the loss of Cu(II) as well as the loss of His44, His118 and His78 indicated by 1HNMR and ESR might be responsible for the mechanism of SOD inactivation; (4) there were great changes in the primary structure and conformation in SOD; (5) the physicochemical properties of SOD were altered; (6) antigenic determinants analysis of SOD was performed and the results showed that there are at least three antigenic determinants in SOD.
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PMID:[Oxidative modification of cupro-zinc superoxide dismutase by reactive oxygen species]. 760 23

The generation of free radicals by Cr(IV) from lipid hydroperoxides was investigated by ESR spin trapping. The spin trap used was 5,5-dimethyl-1-pyrroline N-oxide (DMPO). Reaction of Cr(VI) with ascorbate was used as a source of Cr(IV). Incubation of Cr(VI) with ascorbate generated Cr(IV) and Cr(V). Addition of cumene hydroperoxide generated DMPO/R adduct with an enhancement of Cr(V) signal. Addition of Mn(II), whose function is to remove Cr(IV), caused dose-dependent inhibition of DMPO/R formation. Similar results were obtained using t-butyl hydroperoxide. Metal ion chelators, deferoxamine, 1,10-phenanthroline and diethylenetriaminepentaacetic acid inhibited DMPO/R formation in the order of deferoxamine > 1,10-phenanthroline > diethylenetriaminepentaacetic acid. The results suggest the possible role of Cr(IV) and its mediated free radical generation from lipid hydroperoxides in the mechanism of Cr(VI) carcinogenesis.
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PMID:Generation of free radicals by Cr(IV) from lipid hydroperoxides and its inhibition by chelators. 766 36

Ozone is one of the most potent toxic agents. The noxious effects of its influence on living organisms appear mainly in the lungs and blood. A considerable role in its action is ascribed to free radicals. In this study the ESR method was applied to indirectly demonstrate the free radical effects, as well as the significance of ascorbate in ozonizing the blood. The effects of ozonizing the blood in vitro indicate the existence of a "local" protective mechanism of the blood cells, while in vivo they point out the consumption of ascorbate in "scavenging" of free radicals.
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PMID:Free radical aspects of the ozone influence on blood. 770 Sep 78

While Cr(V) species and .OH radicals have been suggested to play significant roles in the mechanism of chromate-related carcinogenesis, controversy still exists regarding the identity of the Cr(V) species and their role in the generation of .OH radicals. Some recent studies have suggested that the primary Cr(V) species involved is the tetraperoxochromate(V) (CrO8(3-)) ion, which produces .OH radical either on decomposition or by reaction with H2O2. The present study utilized ESR and spin trapping techniques to probe this mechanism. The results obtained show that (i) CrO8(3-) is not formed in any significant quantity in the reaction of chromate with biologically relevant reductants such as glutathione, glutathione reductase, NAD(P)H, ascorbate, vitamin B2, etc. (ii) Decomposition of CrO8(3-), or its reaction with H2O2 does not generate any significant amount of .OH radicals. (iii) The major Cr(V) species formed are complexes of Cr(V) with reductant moieties as ligands. (iv) These Cr(V) complexes generate .OH radicals from H2O2 via Fenton-like reaction. The present study thus disagrees with the recently proposed "tetraperoxochromate(V) theory of carcinogenesis from chromate." Instead, it suggests an alternative mechanism, which might be labeled as "the Cr(V)-complexation-Fenton reaction model of carcinogenesis from chromate.
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PMID:Generation of hydroxyl radical by chromate in biologically relevant systems: role of Cr(V) complexes versus tetraperoxochromate(V). 784 4


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