Purification and Properties of Human Placental ATP Diphosphohydrolase

ATP diphosphohydrolase activity (ATP‐DPH) has been previously identified in the paniculate 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 purificat...

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Veröffentlicht in:	European journal of biochemistry 1995-11, Vol.234 (1), p.66-74
Hauptverfasser:	Christoforidis, Savvas, Papamarcaki, Thomais, Galaris, Dimitrios, Kellner, Roland, Tsolas, Orestes
Format:	Artikel
Sprache:	eng
Schlagworte:	adenosinediphosphatase Affinity Labels Alkaline Phosphatase - metabolism Amino Acid Sequence apyrase Apyrase - antagonists & inhibitors Apyrase - isolation & purification Apyrase - metabolism ATP diphosphohydrolase Chromatography, High Pressure Liquid Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel human placenta Humans Hydrogen-Ion Concentration Molecular Sequence Data photoaffinity labeling Placenta - enzymology Solubility Species Specificity Staining and Labeling
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