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https://olympias.lib.uoi.gr/jspui/handle/123456789/10612Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tselepis, A. D. | en |
| dc.contributor.author | Lekka, M. E. | en |
| dc.contributor.author | Tsoukatos, D. | en |
| dc.date.accessioned | 2015-11-24T16:57:44Z | - |
| dc.date.available | 2015-11-24T16:57:44Z | - |
| dc.identifier.issn | 0014-5793 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10612 | - |
| dc.rights | Default Licence | - |
| dc.subject | platelet-activating factor | en |
| dc.subject | paf | en |
| dc.subject | phospholipase-a2 | en |
| dc.subject | paf-acetylhydrolase | en |
| dc.subject | lipid metabolism | en |
| dc.subject | (tetrahymena-pyriformis) | en |
| dc.subject | platelet-activating-factor | en |
| dc.subject | alkyl ether analog | en |
| dc.subject | acid-labile factor | en |
| dc.subject | 1-o-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine | en |
| dc.subject | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine | en |
| dc.subject | desaturation | en |
| dc.subject | metabolism | en |
| dc.subject | component | en |
| dc.title | A Paf-Acetylhydrolase Activity in Tetrahymena-Pyriformis Cells | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://A1991GD73600035 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/001457939181022Z/1-s2.0-001457939181022Z-main.pdf?_tid=73acdfe17fc0adb63e0f559f081c85f3&acdnat=1333112194_1245a7872eb2f2a5003b4648295dc5c6 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1991 | - |
| heal.abstract | Our study provides evidence for the existence of an acylhydrolase activity in Tetrahymena pyriformis cells, capable of hydrolizing the sn-2 ester bond of the PAF molecule. This activity is mainly distributed in the microsomal fraction (76.5% of total) and has properties similar to the mammalian PAF-acetylhydrolase since it is Ca2+-independent, acid-labile, is inhibited by DFP and PMSF but it is not affected by egg yolk phosphatidylcholine. This microsomal acylhydrolase has apparent K(m) and V(max) values of 1.56-mu-M and 373 pmols . mg . min respectively. This is the first report of the existence of a PAF-acetylhydrolase activity in a non-mammalian cell. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | FEBS Lett | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Tselepis-1991-A Paf-Acetylhydrolas.pdf | 404.5 kB | Adobe PDF | View/Open Request a copy |
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