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. 1979 Jan;63(1):48–52. doi: 10.1104/pp.63.1.48

Inhibition of Adenosine Triphosphatase Activity of the Plasma Membrane Fraction of Oat Roots by Diethylstilbestrol 1

Nelson E Balke a,2, Thomas K Hodges a
PMCID: PMC542763  PMID: 16660690

Abstract

Diethylstibestrol (DES) inhibited noncompetitively the ATPase in the plasma membrane fraction from Avena sativa L. cv. Goodfield roots when assayed in the presence of MgSO4 or MgSO4 plus KCl. In the presence of MgSO4, 7.1×10−5 molar DES inhibited the enzyme 50%; whereas in the presence of MgSO4 and KCl, 1.3×10−4 molar DES was required for the same inhibition. Dixon plots indicated that in the presence of MgSO4, one molecule of DES bound to one molecule of ATPase; however, in the presence of MgSO4 and KCl, two or more molecules bound to one ATPase molecule. These results suggested that KCl causes a conformational change in the enzyme which exposes additional binding sites for DES, but that these sites are not as inhibitory as the first binding site.

In addition to KCl, other factors also affected the DES inhibition of the ATPase. Plasma membrane vesicles warmed to 38 C were inhibited more than vesicles kept on ice prior to assay. DES inhibited the Triton X-100-treated ATPase less than the ATPase which was not detergent-treated. Finally, studies with DES analogs showed that the hydroxyl groups of DES were essential for inhibition and that steric configurations of the molecule were important.

DES inhibition of the ATPase suggests that DES inhibits K+ absorption in oat roots by inhibiting the ATPase. Inhibition of K+ absorption was greater than inhibition of the ATPase, and thus DES may also inhibit other aspects of metabolism that are involved with ion absorption.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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