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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Marselos, M. | en |
| dc.contributor.author | Lindahl, R. | en |
| dc.date.accessioned | 2015-11-24T18:49:59Z | - |
| dc.date.available | 2015-11-24T18:49:59Z | - |
| dc.identifier.issn | 0041-008X | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18024 | - |
| dc.rights | Default Licence | - |
| dc.subject | Aldehyde Dehydrogenase/*biosynthesis | en |
| dc.subject | Animals | en |
| dc.subject | Enzyme Induction | en |
| dc.subject | Kinetics | en |
| dc.subject | Liver/drug effects/*enzymology | en |
| dc.subject | Methylcholanthrene/*pharmacology | en |
| dc.subject | NAD/metabolism | en |
| dc.subject | NADP/metabolism | en |
| dc.subject | Rats | en |
| dc.subject | Tetrachlorodibenzodioxin/pharmacology | en |
| dc.title | Substrate preference of a cytosolic aldehyde dehydrogenase inducible in rat liver by treatment with 3-methylcholanthrene | 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/3420620 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/0041008X88901706/1-s2.0-0041008X88901706-main.pdf?_tid=b0b08a8756c9f7491c781c28996f1ae1&acdnat=1332744239_9ebbe5f900b125f59517319d44ab3ce0 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1988 | - |
| heal.abstract | The substrate preference of an aldehyde dehydrogenase induced in rat liver cytosol by 3-methylcholanthrene was examined. This enzyme, T-ALDH, is identical to the aldehyde dehydrogenase inducible in rat liver by 2,3,7,8-tetrachloro-dibenzo-p-dioxin and the tumor-associated aldehyde dehydrogenase found in rat hepatocellular neoplasms. With either NAD or NADP as coenzyme, the preferred substrates were the aliphatic aldehydes n-hexanal, n-nonanal, and isobutyraldehyde and the aromatic aldehydes 2,5-dihydroxybenzaldehyde, benzaldehyde, and 3-hydroxybenzaldehyde. The results indicate that T-ALDH may play a role in oxidizing a variety of aldehydes produced in physiological lipid metabolism. On the contrary, this isozyme does not seem to participate in the oxidation of small aliphatic aldehydes generated during lipid peroxidation. Similarly, no significant activity could be detected when the enzyme was tested with aldehydes produced in carbohydrate, amino acid, polyamine, steroid, and vitamin metabolism. | en |
| heal.journalName | Toxicol Appl Pharmacol | 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 | |
|---|---|---|---|---|
| Marselos-1988-Substrate preference.pdf | 620.47 kB | Adobe PDF | View/Open Request a copy |
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