Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.3 (ascorbate oxidase)
 778 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzymic memory is a kinetic phenomenon observable in double displacement mechanisms. The defining feature of enzymic memory is the occurrence of different rates of transfer for a common transferable group from the substituted enzymes obtained with different donor substrates. Memory behavior was previously demonstrated for both the bovine and human liver rhodaneses (EC 2.8.1.1). Steady state kinetic tests for enzymic memory have now been done with ascorbate oxidase (EC 1.10.3.3) and aspartate aminotransferase (EC 2.6.1.1). The results were positive with ascorbate oxidase, which showed an oxygen reactivity ratio of 1:20:300 for the reduced enzymes obtained with reductate, araboascorbate, and ascorbate, respectively. Results were negative for the aminotransferase tested with the alternate donors glutamate and cysteine sulfinate, with oxaloacetate as the common acceptor. The structural basis of the ascorbate oxidase results was probed by comparison of both the ultraviolet absorption and fluorescence spectra of the oxidized enzyme with those of the reduced forms obtained with ascorbate and reductate. The results are consistent with a conformational basis for the memory phenomenon.
J Biol Chem 1979 Sep 25
PMID:Enzymic memory. Steady state kinetic and physical studies with ascorbate oxidase and aspartate aminotransferase. 47 84

The antithyroid drug, methimazole (1-methyl-2-thiolimidazole), is a powerful chelator of cupric ion. This is reflected in its ability to selectively inhibit certain copper oxidases. Uricase, ascorbic oxidase and monoamine oxidase are not affected. Ceruloplasmin oxidase is slightly inhibited and tyrosinase is markedly inhibited by methimazole.
Experientia 1975 Sep 15
PMID:Copper ion binding and enzyme inhibitory properties of the antithyroid drug methimazole. 80 93

This report examines the effect of the endolymphatic shunt on hearing. The study group was drawn from 101 shunt operations for intractable vertigo between 1983 and 1987. Thirty ears met criteria for diagnosis, level of preoperative hearing impairment, and length of follow-up. The control group consisted of 30 ears with symptoms severe enough to prompt recommendations for shunt surgery, but the patients either opted against surgery or improved. The results were analyzed using the 1985 AAO-HNS reporting criteria. When looking at worst postoperative (or worst scores after 2 years of follow-up in controls) compared to worst preoperative (or worst scores in the first 6 months of presentation in controls), we found no significant difference between the study group (average loss of 9 dB pure-tone average [PTA] and 16% speech discrimination [SD]) as compared to the control group (average loss of 3 dB PTA and 10% SD). However, when using the first and last audiograms for the control group, there was a statistically significant difference as compared to the worst preoperative and postoperative scores in the shunt group. Using the first and last scores, the control group had a better outcome (PTA improved 2 dB, SD score dropped 5%). There was no significant difference between groups for percentage of patients whose hearing improved, remained the same, or worsened. In conclusion, the endolymphatic shunt operation did not significantly effect the long-term hearing results.
Am J Otol 1992 Sep
PMID:Hearing results from endolymphatic sac surgery. 144 73

Anaerobic reduction kinetics of the zucchini squash ascorbate oxidase (AO; L-ascorbate:oxygen oxidoreductase, EC 1.10.3.3) by pulse radiolytically produced CO2- radical ions were investigated. Changes in the absorption bands of type 1 [Cu(II)] (610 nm) and type 3 [Cu(II)] (330 nm) were monitored over a range of reactant concentrations, pH, and temperature. The direct bimolecular reduction of type 1 [Cu(II)] [(1.2 +/- 0.2) x 10(9) M-1.s-1] was followed by its subsequent reoxidation in three distinct phases, all found to be unimolecular processes with the respective specific rates of 201 +/- 8, 20 +/- 4, and 2.3 +/- 0.2 s-1 at pH 5.5 and 298 K. While at this pH no direct bimolecular reduction was resolved in the 330-nm band, at pH 7.0 such a direct process was observed [(6.5 +/- 1.2) x 10(8) M-1.s-1]. In the same slower time domains where type 1 [Cu(I)] reoxidation was monitored, reduction of type 3 [Cu(II)] was observed, which was also concentration independent and with identical rate constants and amplitudes commensurate with those of type 1 [Cu(II)] reoxidation. These results show that after electron uptake by type 1 [Cu(II)], its reoxidation takes place by intramolecular electron transfer to type 3 [Cu(II)]. The observed specific rates are similar to values reported for the limiting-rate constants of AO reduction by excess substrate, suggesting that internal electron transfer is the rate-determining step of AO activity. The temperature dependence of the intramolecular electron transfer rate constants was measured from 275 to 308 K at pH 5.5 and, from the Eyring plots, low activation enthalpies were calculated--namely, 9.1 +/- 1.1 and 6.8 +/- 1.0 kJ.mol-1 for the fastest and slowest phases, respectively. The activation entropies observed for these respective phases were -170 +/- 9 and -215 +/- 16 J.K-1.mol-1. The exceptionally low enthalpy barriers imply the involvement of highly optimized electron transfer pathways for internal electron transfer.
Proc Natl Acad Sci U S A 1992 Sep 01
PMID:Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase. 151 59

Based on the novel chromophoric electron donors, N,N-dimethyl-1,4-phenylenediamine (DMPD) and 2-amino-2-deoxy-L-ascorbic acid (2-aminoascorbic acid), two sensitive, convenient, and continuous spectrophotometric assays for dopamine beta-monooxygenase (EC 1.14.17.1) are described. Both, DMPD and 2-aminoascorbic acid are kinetically and stoichiometrically well-behaved electron donors for dopamine beta-monooxygenase with kinetic parameters comparable to the most efficient physiological electron donor, ascorbic acid. During dopamine beta-monooxygenase turnover, DMPD is converted to its chromophoric cation radical which is stable under the standard assay conditions. The rate of the enzyme-dependent formation of DMPD cation radical under standard assay conditions could easily be followed at 515 nm with high accuracy and reproducibility. Similarly, dopamine beta-monooxygenase-mediated oxidation of 2-aminoascorbic acid results in the formation of the known, stable chromophoric product, 2,2'-nitrilodi-2(2')-deoxy-L-ascorbic acid (red pigment), which has a very strong absorption maximum at 385 nm. Both the above assays are superior to the existing assays in their convenience, reproducibility, and sensitivity for routine kinetic analysis of dopamine beta-monooxygenase and may be adopted as a simple color test for the enzyme. We propose that the above assays could also be adopted to design continuous and sensitive spectrophotometric assays for ascorbate oxidase, peptidyl alpha-amidating monooxygenase, and the chromaffin granule electron transport protein, cytochrome b561, due to their remarkable similarity to dopamine beta-monooxygenase in the chemistry of catalysis with regard to the electron donor.
Anal Biochem 1991 Sep 02
PMID:Continuous spectrophotometric assays for dopamine beta-monooxygenase based on two novel electron donors: N,N-dimethyl-1,4-phenylenediamine and 2-aminoascorbic acid. 178 90

Chromium (VI) reductase activity was measured in ultrafiltrates of rat liver and kidney after various pretreatments in vitro at 37 degrees C and pH 7.0. Preincubation of ultrafiltrates with L-ascorbate oxidase (EC 1.10.3.3), which specifically eliminated ascorbate, blocked approximately 80% of the Cr(VI) reductase activity. Heat-denatured ascorbate oxidase had no effect on Cr(VI) reductase activity in ultrafiltrates. Preincubation of ultrafiltrates with N-ethylmaleimide, which non-specifically blocked sulfhydryls, including reduced glutathione, decreased Cr(VI) reductase activity by only 20%. Treatment of male Sprague-Dawley rats with phorone decreased non-protein sulfhydryl (NPSH) levels in rat liver by greater than 90% and tripled reduced ascorbate levels 2 h after treatment. Ultrafiltrates of liver prepared from phorone-treated rats had twice the Cr(VI) reductase activity of control ultrafiltrates, and greater than 95% of this activity could be blocked by preincubation with ascorbate oxidase. Treatment of rats with sodium dichromate (20 mg/kg) caused a significant decrease in ascorbate levels in kidney but not liver, and no change in NPSH levels in kidney or liver, 15 min after treatment. We conclude that ascorbate is the major reductant of Cr(VI) in rat liver and kidney ultrafiltrates and may well be the major non-enzymatic reductant of Cr(VI) in rat liver and kidney in vivo.
Carcinogenesis 1991 Sep
PMID:Ascorbate is the principal reductant of chromium (VI) in rat liver and kidney ultrafiltrates. 189 33

A highly sensitive flavin adenine dinucleotide-3'-phosphate (FADP)-based enzyme amplification cascade has been developed for determining alkaline phosphatase (ALP; EC 3.1.3.1). The cascade detects ALP via the dephosphorylation of the novel substrate FADP to produce the cofactor FAD, which binds stoichiometrically to inactive apo D-amino acid oxidase (D-AAO). The resulting active holo D-AAO oxidizes D-proline to produce hydrogen peroxide, which is quantified by the horseradish peroxidase-mediated conversion of 3,5-dichloro-2-hydroxybenzenesulfonic acid and 4-aminoantipyrine to a colored product. The FADP-based enzyme amplification cascade has been used in a novel releasable linker immunoassay (RELIA) to quantify thyrotropin (TSH). In the assay, TSH is first captured onto antibody-coated chromium dioxide particles. After formation of an antibody-TSH sandwich with a dethiobiotinylated second antibody, the complex is reacted with a streptavidin-ALP conjugate. Biotin is then used to release the conjugate into solution, and ALP is quantified in an automated version of the FADP-based amplification cascade on the aca discrete clinical analyzer (Du Pont). The sensitivity of the colorimetric RELIA assay for TSH (less than 0.1 milli-int. unit/L) is comparable with that of fluorometric assays. This technology provides a way to adapt to the aca high-sensitivity immunoassays for a wide range of analytes via colorimetric detection.
Clin Chem 1991 Sep
PMID:Sensitive, colorimetric enzyme amplification cascade for determination of alkaline phosphatase and application of the method to an immunoassay of thyrotropin. 189 77

In minced meat products, ascorbic acid interferes in the usual spectrophotometric determination of nitrite by the diazotisation-coupling technique with sulphanilamide and N-(1-naphthyl)ethylenediamine. In a modified extraction method, the enzyme ascorbate oxidase was shown to diminish the interference of the acid. Within 10 min the enzyme was able to reduce the level of ascorbic acid in the minced meat specimens from 1000 p.p.m. down to the tolerance limit for interference. This appeared to be superior to the extraction method involving the use of water and was comparable to a previously described method based on the use of 0.01 M sodium hydroxide. As isoascorbic acid is not approved as a food additive in Norway no attempt was made to investigate the influence of this acid.
Analyst 1990 Sep
PMID:Improved extraction method for avoiding the interference of ascorbic acid in the spectrophotometric determination of nitrite in meat products. 209 97

In an attempt to decrease ascorbate interference on the ion-chromatographic determination of urinary oxalate, we compared the effectiveness of four different methods for ascorbate elimination by analyzing a representative urine pool supplemented with successive ascorbate additions. Two of the methods--treatment with ferric ions or boric acid--have been described elsewhere; treatments with nitrites or ascorbate oxidase (EC 1.10.3.3) are investigated here as possible alternatives. Consideration of the main features, advantages, and drawbacks of the four procedures leads us to conclude that boric acid dilution is a good routine method and that pre-incubation with ascorbate oxidase reliably prevents ascorbate interference in assays of urinary oxalate.
Clin Chem 1990 Sep
PMID:Preventing ascorbate interference in ion-chromatographic determinations of urinary oxalate: four methods compared. 220 5

This issue of The American Journal of Otology includes the last of a series of articles on facial nerve disorders, which collectively are known as the "Facial Nerve Manual." In the early 1980s, Dr. Mark May chaired the AAO-HNS Facial Nerve Committee. One of the tasks he initiated was the creation of a Facial Nerve Manual, assigned to a small group of clinicians at the COSM Meeting in the spring of 1984. The purpose of this work was to disseminate practical information on the management of selected facial nerve problems, one of the primary charges of the Committee. Work began slowly, but surely. During Dr. Gale Gardner's tenure as Committee chairman, manuscripts were reviewed and edited by Dr. Nels Olson, and The American Journal of Otology agreed to publish the manual. Perhaps more than anyone else, Dr. Olson worked tirelessly to create a finished product of consistent style and content. Ever since the original writing and editing, controversial topics continue to emerge. As each chapter is published individually over this year, concepts may change, and the reader is encouraged to explore these issues in more depth. Drs. May, Gardner, Olson, and all the individual authors are to be congratulated for their efforts. The Committee sincerely thanks The American Journal of Otology for supporting this work.
Am J Otol 1989 Sep
PMID:Pathophysiology of facial nerve disorders. 268 5


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