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Am J Physiol Renal Physiol 278: F978-F988, 2000;
0363-6127/00 $5.00
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Vol. 278, Issue 6, F978-F988, June 2000

Purification, characterization, and localization of an ATP diphosphohydrolase in porcine kidney

Raf Lemmens1, Luc Kupers1, Jean Sévigny2, Adrien R. Beaudoin3, Gilles Grondin3, Agnes Kittel4, Etienne Waelkens5, and Luc Vanduffel1

1 Department Medische BasisWetenschappen, Limburgs Universitair Centrum, B-3590 Diepenbeek, Belgium; 2 Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215; 3 Département de Biologie, Université de Sherbrooke, Sherbrooke, Québec, Canada J1K 2R1; 4 Institute of Experimental Medicine, H-1450 Budapest, Hungary; and 5 Biochemie, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium

Membranes of pig kidney cortex tissue were solubilized in the presence of Triton X-100. Partial purification of ATP diphosphohydrolase (ATPDase) was achieved by successive chromatography on concanavalin A-Sepharose, Q-Sepharose Fast Flow, and 5'-AMP-Sepharose 4B. Monoclonal antibodies against ATPDase were generated. Further purification of the ATPDase was obtained by immunoaffinity chromatography with these monoclonal antibodies. NH2-terminal amino acid sequencing of the 78-kDa protein showed a sequence very homologous to mammalian CD39. The protein is highly glycosylated, with a nominal molecular mass of ~57 kDa. The purified enzyme hydrolyzed di- and triphosphates of adenosine, guanosine, cytidine, uridine, inosine, and thymidine, but AMP and diadenosine polyphosphates could not serve as substrates. All enzyme activities were dependent on divalent cations and were partially inhibited by 10 mM sodium azide. The distribution of the enzyme in pig kidney cortex was examined immunohistochemically. The enzyme was found to be present in blood vessel walls of glomerular and peritubular capillaries.

CD39; apyrase; nucleoside triphosphate diphosphohydrolase; Triton X-100


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