Human placental ATP diphosphohydrolase is a highly N-glycosylated plasma membrane enzyme
| dc.contributor.author | Christoforidis, S. | en |
| dc.contributor.author | Papamarcaki, T. | en |
| dc.contributor.author | Tsolas, O. | en |
| dc.date.accessioned | 2015-11-24T19:12:55Z | |
| dc.date.available | 2015-11-24T19:12:55Z | |
| dc.identifier.issn | 0006-3002 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/21132 | |
| dc.rights | Default Licence | - |
| dc.subject | Amidohydrolases/metabolism | en |
| dc.subject | Apyrase/*metabolism | en |
| dc.subject | Cell Membrane/*enzymology | en |
| dc.subject | Electrophoresis, Polyacrylamide Gel | en |
| dc.subject | Female | en |
| dc.subject | Glycoside Hydrolases/metabolism | en |
| dc.subject | Glycosylation | en |
| dc.subject | Humans | en |
| dc.subject | Hydrogen-Ion Concentration | en |
| dc.subject | Molecular Weight | en |
| dc.subject | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase | en |
| dc.subject | Placenta/*enzymology | en |
| dc.subject | Pregnancy | en |
| dc.title | Human placental ATP diphosphohydrolase is a highly N-glycosylated plasma membrane enzyme | en |
| heal.abstract | Human placental ATP diphosphohydrolase (ATP-DPH), has been previously characterized as an azide-sensitive, Ca(2+)- or Mg(2+)-dependent triphospho- and diphosphonucleosidase which migrates as an 82 kDa protein band on SDS-PAGE (Christoforidis, S. et al. (1995) Eur. J. Biochem. 234, 66-74). In this paper we have studied the subcellular localization of placental ATP-DPH by differential centrifugation and flotation experiments. Using specific enzymatic markers it was found that ATP-DPH is localized on plasma membrane. ATP-DPH was found to be a highly N-glycosylated protein which is a common post-translational modification of plasma membrane proteins. Extensive incubation of the native pure enzyme with N-glycosidase F resulted in the elimination of the 82 kDa form and the concurrent formation of a deglycosylated product of 57.5 kDa and four other intermediate products, indicating the presence of at least five N-glycosylation sites within the ATP-DPH molecule. The partially deglycosylated sample retained its activity in solution and in native gel electrophoresis and activity staining. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/8703981 | - |
| heal.journalName | Biochim Biophys Acta | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1996 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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