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ATPase activity of pharmacological preparations

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Abstract

The ATPase activity of pharmacological preparations was tested in phosphate buffer to determine if the breakdown products of ATP contribute significantly to the responses observed to externally applied ATP. Large masses of tissues rapidly broke down ATP whereas the arterial preparations were the most active per unit mass.

References (10)

  • L.G. Abood et al.

    Biochim. Biophys. Acta

    (1968)
  • P. Hrdina et al.

    European J. Pharmacol.

    (1967)
  • R. Parvin et al.

    Anal. Biochem.

    (1969)
  • J.G. Allen et al.

    Arch. Intern. Pharmacodyn.

    (1970)
  • J. Axelsson et al.

    Acta Physiol. Scand.

    (1969)
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    2014, Journal of Biological Chemistry
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    We showed here that NTPDase1 deletion leads to an important reduction in the hydrolytic activity at the surface of vas deferens SMCs, especially at low micromolar concentrations of ATP. These data demonstrate that NTPDase1 is the high-affinity enzyme responsible for the main ATPase activity reported previously in this tissue (30) which is also in agreement with the immunolocalization of NTPDase1 in the vas deferens (19). NTPDase1 has been described in virtually all vascular and visceral SMCs (14, 19, 31, 32), making this enzyme the key ectonucleotidase in the regulation of P2 receptor activation on these cells and, consequently, purinergically dependent smooth muscle contraction.

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