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Ecto-ATPase Activity in the Kidney

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Ecto-ATPases

Abstract

The first mention of renal ATPase activities, stimulated by Ca2+- or Mg2+-ions and different from the well-described Na+,K+-ATPase in the kidney, appeared during the sixties.

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References

  1. K.P. Wheeler and R. Whittam, 1964. Structural and enzymic aspects of the hydrolysis of adenosine triphosphate by membranes of kidney cortex and erythrocytes, Biochem. J. 93: 349–363.

    PubMed  CAS  Google Scholar 

  2. D.K. Parkinson and I.C. Radde, 1971. Properties of Ca2+-and Mg2+-activated ATP-hydrolyzing enzyme in rat kidney cortex, Biochim. Biophys. Acta 242: 238–246.

    Article  PubMed  CAS  Google Scholar 

  3. G. Rorive and A. Kleinzeller, 1972. The effect of ATP and Ca2+ on the cell volume in isolated kidney tubulues, Biochim. Biophys. Acta 274: 226–239.

    Article  PubMed  CAS  Google Scholar 

  4. E. Kinne-Saffran and R. Kinne, 1974. Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex, J. Membr. Biol. 17: 263–274.

    Article  PubMed  CAS  Google Scholar 

  5. M.L. Gantzer and C.M. Grisham, 1979. Characterization of Mg2+-ATPase from sheep kidney medulla: Purification, Arch. Biochem. Biophys. 198(1): 263–267.

    Article  PubMed  CAS  Google Scholar 

  6. M. Mörtl, D. Busse, H. Bartel, and B. Pohl, 1984. Partial purification and characterization of rabbit-kidney brush-border (Ca2+or Mg2+)-dependent adenosine triphosphatase, Biochim. Biophys. Acta 776: 237–246.

    Article  PubMed  Google Scholar 

  7. I. Ilsbroux, L. Vanduffel, H. Teuchy, and M. De Cuyper, 1985. An azide-insensitive low-affinity ATPase stimulated by Ca2+ or Mg2+ in basal-lateral and brush border membranes of kidney cortex, Eur. J. Biochem. 151:123–129.

    Article  PubMed  CAS  Google Scholar 

  8. M. Van Erum, L. Martens, L. Vanduffel, and H. Teuchy, 1988. The localization of (Ca2+ or Mg2+)-ATPase in plasma membranes of renal proximal tubular cells, Biochim. Biophys. Acta 937: 145–152.

    Article  PubMed  Google Scholar 

  9. M. Van Erum, R. Lemmens, J. Berden, H. Teuchy, and L. Vanduffel, 1995. Identification and partial purification of (Ca2+ or Mg2+)-ATPase in renal brush-border membranes, Eur. J. Biochem. 227: 150–160.

    Article  PubMed  Google Scholar 

  10. K. Yagi, Y. Arai, N. Kato, K. Hirota and, Y. Miura, 1989. Purification of ATP diphosphohydrolase from bovine aorta microsomes, Eur. J. Biochem. 180: 509–513.

    Article  PubMed  CAS  Google Scholar 

  11. F.D.L. Moodie, H. Baum, P.J. Butterworth, and T.J. Peters, 1991. Purification and characterization of bovine spleen ADPase, Eur J. Biochem. 202: 1209–1215.

    Article  PubMed  CAS  Google Scholar 

  12. M.J. Treuheit, P.L. Vaghy, and T.L. Kirley, 1992. Mg2+-ATPase from rabbit skeletal muscle transverse tubules is 67-kilodalton glycoprotein, J. Biol. Chem. 267(17): 11777–11782.

    PubMed  CAS  Google Scholar 

  13. J.G. Stout and T.L. Kirley, 1994. Purification and acharacterization of the ecto-ATPase of chicken gizzard smooth muscle, J. Biochem. Biophys. Methods 29: 61–75.

    Article  PubMed  CAS  Google Scholar 

  14. J. Sevigny, Y.P. Côté, and A.R. Beaudoin, 1995. Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5′-p fluorosulphonylbenzoyladenosine ATP analogue, Biochem. J. 312: 351–356.

    PubMed  CAS  Google Scholar 

  15. S. Christoforidis, T. Papamarcaki, D. Galaris, R. Kellner, and O. Tsolas, 1995. Purification and properties of human placental ATP diphosphohydrolase, Eur. J. Biochem. 234: 66–74.

    Article  PubMed  CAS  Google Scholar 

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Vanduffel, L., Lemmens, R., Teuchy, H. (1997). Ecto-ATPase Activity in the Kidney. In: Plesner, L., Kirley, T.L., Knowles, A.F. (eds) Ecto-ATPases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5955-9_12

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  • DOI: https://doi.org/10.1007/978-1-4615-5955-9_12

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7729-0

  • Online ISBN: 978-1-4615-5955-9

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