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5 Beta,14 beta-androstane-3 beta,14-diol binds to the digitalis receptor site on Na/K-ATPase
W Schönfeld1, K H Menke, R Schönfeld
1Central Institute of Molecular Biology, Academy of Sciences, G.D.R., Berlin.
Journal of Enzyme Inhibition
|January 1, 1987
Abstract:
5 beta,14 beta-Androstane-3 beta,-14-diol, the lead (minimum) structure in digitalis compounds, shows the same characteristics of interaction with Na/K-ATPase as ordinary digitalis compounds judged by the following six criteria: (I) shape of the concentration-inhibition curves, (II) species differences in affinity for the enzyme, (III) apparent competition with K+, (IV) competition with digitoxigenin for binding to the enzyme, (V) stabilization of phosphoenzyme formed from ATP, and (VI) enhancement of phosphorylation from orthophosphate.