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Chelation of mercury by ouabain-sensitive and ouabain-resistant renal Na,K-ATPase
B M Anner1, M Moosmayer, E Imesch
1Department of Pharmacology, Geneva University Medical Center, Switzerland.
Biochemical and Biophysical Research Communications
|March 30, 1990
Abstract:
The SH-reactive HgCl2 inhibits the Na,K-ATPase activity potently in a manner antagonized only partially by EDTA or cysteine; solely dimercaprol, a dithiol antidote for mercury, blocks the HgCl2 effects entirely as confirmed also by 203Hg-binding experiments. The results reveal the presence of a chelating component in pure Na,K-ATPase with an affinity for mercury superior to EDTA. The mercury-sensitivity of the Na,K-ATPase is not related to the ouabain-sensitivity. This criterion will be useful for the distinction between ouabain-like and mercury-like inhibitors from body fluids and tissues.