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DC Field | Value | Language |
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dc.contributor.author | Tellis, C. | en |
dc.contributor.author | Pantazi, D. | en |
dc.contributor.author | Ioachim, E. | en |
dc.contributor.author | Galani, V. | en |
dc.contributor.author | Lekka, M. E. | en |
dc.date.accessioned | 2015-11-24T16:41:11Z | - |
dc.date.available | 2015-11-24T16:41:11Z | - |
dc.identifier.issn | 0171-9335 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8379 | - |
dc.rights | Default Licence | - |
dc.subject | tetrahymena pyriformis | en |
dc.subject | nadph-cytochrome c reductase | en |
dc.subject | succinate dehydrogenase | en |
dc.subject | paf | en |
dc.subject | cholinephosphotransferase | en |
dc.subject | platelet-activating-factor | en |
dc.subject | cytochrome-c reductase | en |
dc.subject | mitochondria | en |
dc.subject | membrane | en |
dc.subject | stimulation | en |
dc.subject | enzymes | en |
dc.subject | cells | en |
dc.subject | acid | en |
dc.subject | paf | en |
dc.title | Localization of an alkyl-acetyl-glycerol-CDP-choline : cholinephosphotransferase activity in submitochondrial fractions of Tetrahymena pyriformis | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.secondary | <Go to ISI>://000187637800005 | - |
heal.identifier.secondary | http://ac.els-cdn.com/S0171933504703295/1-s2.0-S0171933504703295-main.pdf?_tid=67aaa81651fe01a401302d5e7dd61334&acdnat=1333034084_4a72ea5b60e8dff0442d232d830916ea | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 2003 | - |
heal.abstract | Tetrahymena pyriformis contains platelet-activating factor (PAF) as a minor lipid, which is biosynthesized de novo. A dithiothreitoll-insensitive CDP-choline:cholinephospotransferase (AAG-CPT), which utilizes alkyl-acetyl-glycerol as a substrate, had been detected in both the mitochondrial and microsomal fractions of the protozoan. In the present report, localization of this enzyme in submitochondrial fractions was studied. Cell fractionation was evaluated with enzyme and morphological markers. In this respect, succinate dehydrogenase, NADPH:cytochrome c reductase, glucose-6-phosphatase, alkaline phosphatase, monoaminoxidase, and cytochrome c oxidase activities were investigated. In the presence of antimycin A, mitochondrial activity of NADPH-cytochrome c reductase, was increased, while the microsomal one was reduced. Cardiolipin was distributed in the inner mitochondrial membrane. Alkaline phosphatase was found exclusively in the cytosol of the protozoan. The main portion of the dithiothreitoll-insensitive AAG-CPT was localized in the inner mitochondrial membrane. Our data indicate that mitochondria are able to produce PAF, which might be associated with their function. | en |
heal.publisher | Elsevier | en |
heal.journalName | Eur J Cell Biol | 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 | |
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Tellis-2003-Localization of an a.pdf | 161.01 kB | Adobe PDF | View/Open Request a copy |
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