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https://olympias.lib.uoi.gr/jspui/handle/123456789/10356Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tellis, C. | en |
| dc.contributor.author | Lekka, M. E. | en |
| dc.date.accessioned | 2015-11-24T16:55:47Z | - |
| dc.date.available | 2015-11-24T16:55:47Z | - |
| dc.identifier.issn | 1066-5234 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10356 | - |
| dc.rights | Default Licence | - |
| dc.subject | alkyl-acetyl-glycerophosphate : phosphohydrolase paf | en |
| dc.subject | phosphatidate phosphohydrolase | en |
| dc.subject | phospholipase a(2) | en |
| dc.subject | phospholipase c | en |
| dc.subject | phospholipid biosynthesis | en |
| dc.subject | platelet-activating-factor | en |
| dc.subject | phosphatidate phosphohydrolase | en |
| dc.subject | rat-liver | en |
| dc.subject | subcellular-distribution | en |
| dc.subject | biosynthesis | en |
| dc.subject | fractions | en |
| dc.subject | purification | en |
| dc.subject | yeast | en |
| dc.subject | cells | en |
| dc.subject | assay | en |
| dc.title | 1-O-alkyl-2-acetyl-sn-glycero-3-phosphate : phosphohydrolase activity in Tetrahymena pyriformis | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000086049500003 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1111/j.1550-7408.2000.tb00021.x/asset/j.1550-7408.2000.tb00021.x.pdf?v=1&t=h0dxyth1&s=91ef864cd08d7f819f6c127e182f7f7a190bbed0 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2000 | - |
| heal.abstract | Within the frame of the de novo formation of Platelet-Activating Factor in Tetrahymena, the occurrence as well as the properties of a lipid phosphate phosphohydrolase activity catalyzing the dephosphorylation of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphate was investigated. The activity was distributed in all the membrane fractions of the cell and in the cytosol. It showed preference for acyl-acetyl-sn-glycero-phosphate as well, and at a much lower level, for dipalmitoyl-glycero-phosphate. Mg2+ and Ca2+ caused a dose-dependent inhibition, while F-, EDTA and EGTA had no effect. The enzymic activity was linear for at least up to 60 min incubation time and up to 150 mu g protein. Microsomal activity exhibited two optimal pH areas, around 7.0 and 9.0, while mitochondrial activity showed one peak, at pH 7.0. Acyl-GP, acyl-acetyl-GP and alkyl-GP could replace alkyl-acetyl-GP in significant rates, while dipalmitoyl-GP, beta-GP, fructose-6-GP, p-nitrophenylphosphate, creatine phosphate or ATP had no effect. Side phospholipose A(2) and C activities were also detected. Taking into account the presence of PAF and alkylacetylglycerol in the protozoan as well as the presence of a dithiothreitol- insensitive CDP-choline:cholinephosphotransferase activity that converts alkylacetylglycerol to PAF, we suggest that the present phosphohdrolase activity may be involved in the de novo production of PAF within Tetrahymena. | en |
| heal.publisher | Wiley-Blackwell | en |
| heal.journalName | Journal of Eukaryotic Microbiology | 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 | |
|---|---|---|---|---|
| Tellis-2000-1-O-alkyl-2-acetyl-s.pdf | 849.06 kB | Adobe PDF | View/Open Request a copy |
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