Purification and characterization of human urine-derived digitalis-like factor

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Abstract

We were able to purify a digitalis-like factor to apparent homogeneity from human urine based on the inhibitory effect on [3H]-ouabain binding to intact human erythrocytes. This ouabain displacing compound closely resembles ouabain in its polarity, molecular weight, non-peptidic nature and mode of action except for its UV absorbance spectrum. This compound sharing many biological activities of ouabain may be the endogenous ligand for the Na+, K+-ATPase and serve as a specific regulator of the sodium pump.

References (17)

  • A. Goto et al.

    Biochem. Biophys. Res. Comm

    (1988)
  • H.W. Jarrett et al.

    J. Biol. Chem

    (1978)
  • K. Inui et al.

    Biochem. Biophys. Res. Comm

    (1985)
  • M. Tamura et al.

    Biochem. Biophys. Res. Comm

    (1987)
  • F.J. Haddy

    N. Eng. J. Med

    (1987)
  • L. Poston

    Clin. Sci

    (1987)
  • S.W. Graves et al.

    Ann. Rev. Med

    (1987)
  • H. Haber et al.

    Hypertension

    (1987)
There are more references available in the full text version of this article.

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