Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/19636Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Galaris, D. | en |
| dc.contributor.author | Korantzopoulos, P. | en |
| dc.date.accessioned | 2015-11-24T19:01:02Z | - |
| dc.date.available | 2015-11-24T19:01:02Z | - |
| dc.identifier.issn | 0891-5849 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/19636 | - |
| dc.rights | Default Licence | - |
| dc.subject | Acetylation | en |
| dc.subject | Animals | en |
| dc.subject | Ascorbic Acid/*pharmacology | en |
| dc.subject | Free Radicals/metabolism | en |
| dc.subject | Horses | en |
| dc.subject | Hydrogen Peroxide/*metabolism/pharmacology | en |
| dc.subject | Kinetics | en |
| dc.subject | Metmyoglobin/drug effects/*metabolism | en |
| dc.subject | Muscles/injuries/metabolism | en |
| dc.subject | Oxidation-Reduction | en |
| dc.subject | Oxidative Stress | en |
| dc.subject | Reactive Oxygen Species/metabolism | en |
| dc.subject | Tyrosine/metabolism | en |
| dc.title | On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/9013128 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0891584996003826/1-s2.0-S0891584996003826-main.pdf?_tid=48c9dd6c5a02b96a0982b481a3a8b272&acdnat=1333963070_675e3eeff5c2dcb8ee9fe43f01cfa44d | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1997 | - |
| heal.abstract | Hydrogen peroxide induces rapid oxidation of metmyoglobin with an apparent second order rate constant, k1 = 3.4 x 10(4) M-1 min-1. The product of this interaction is ferrylmyoglobin with an unstable free radical on the globin moiety. This activated form of myoglobin is able: (a) to initiate the peroxidation of erythrocyte membranes and (b) to form intra- and intermolecular covalent crosslinkings. The presence of ascorbic acid in amounts stoichiometric to H2O2 efficiently prevents all the above processes. Moreover, in the presence of ascorbic acid a cyclic process is taking place leading to H2O2 reduction, ascorbic acid oxidation, and unmodified metmyoglobin formation (reaction 1). | en |
| heal.journalName | Free Radic Biol Med | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Galaris-1997-On the molecular mec.pdf | 385.57 kB | Adobe PDF | View/Open Request a copy |
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