| http://purl.uniprot.org/citations/8529670 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8529670 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8529670 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/8529670 | http://www.w3.org/2000/01/rdf-schema#comment | "ATP diphosphohydrolase activity (ATP-DPH) has been previously identified in the particulate fraction of human term placenta [Papamarcaki, T. & Tsolas, O. (1990) Mol. Cell. Biochem. 97, 1-8]. In the present study we have purified to homogeneity and characterized this activity. A 260-fold purification has been obtained by solubilization of the particulate fraction and subsequent chromatography on DEAE Sepharose CL-6B and 5'-AMP Sepharose 4B. The preparation has been shown to be free of alkaline phosphatase even though the placental extract is rich in this activity. The purified enzyme is a glycoprotein and migrates as a single broad band of 82 kDa on SDS/PAGE. The same band is obtained after photoaffinity labeling of the enzyme with 8-azido-[alpha-32P]ATP. The enzyme has a broad substrate specificity, hydrolyzing triphosphonucleosides and diphosphonucleosides but not monophosphonucleosides or other phosphate esters. The activity is dependent on the addition of divalent cations Ca2+ or Mg2+. The Km values for ATP and ADP were determined to be 10 microM and 20 microM, respectively. Maximum activity was found at pH 7.0-7.5 with ATP as substrate, and pH 7.5-8.0 with ADP. The enzymic activity is inhibited by NaN3, NaF, adenosine 5'-[beta,gamma-imido]triphosphate and adenosine 5'-[alpha,beta-methylene]triphosphate. Protein sequence analysis showed ATP-DPH to be N-terminally blocked. Partial internal amino acid sequence information was obtained after chymotryptic cleavage and identified a unique sequence with no significant similarity to known proteins. ATP-DPH activity has been reported to be implicated in the prevention of platelet aggregation, hydrolysing ADP to AMP and thus preventing blood clotting."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1995.066_c.x"xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1995.066_c.x"xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Kellner R."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Kellner R."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Christoforidis S."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Christoforidis S."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Tsolas O."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Tsolas O."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Galaris D."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Galaris D."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Papamarcaki T."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/author | "Papamarcaki T."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/pages | "66-74"xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/pages | "66-74"xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/title | "Purification and properties of human placental ATP diphosphohydrolase."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/title | "Purification and properties of human placental ATP diphosphohydrolase."xsd:string |
| http://purl.uniprot.org/citations/8529670 | http://purl.uniprot.org/core/volume | "234"xsd:string |