Human placental ATP diphosphohydrolase is a highly N-glycosylated plasma membrane enzyme
| Autor: | Orestes Tsolas, Savvas Christoforidis, Thomais Papamarcaki |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Placenta/*enzymology
Glycosylation Glycoside Hydrolases Placenta Apyrase/*metabolism Biophysics Biology Cell Membrane/*enzymology Biochemistry Amidohydrolases Glycoside Hydrolases/metabolism Pregnancy Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Glycoside hydrolase Incubation Differential centrifugation chemistry.chemical_classification Subcellular localization Apyrase Cell Membrane ADPase Cell Biology Hydrogen-Ion Concentration Molecular biology Staining Amidohydrolases/metabolism Molecular Weight Enzyme Membrane chemistry Membrane protein Human placenta Electrophoresis Polyacrylamide Gel Female lipids (amino acids peptides and proteins) ATP diphosphohydrolase Deglycosylation |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1282:257-262 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/0005-2736(96)00065-x |
| Popis: | 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. Biochim Biophys Acta |
| Databáze: | OpenAIRE |
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