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Interaction of Anthraquinones with Nucleotide Binding Site of Na+,K+-ATPase

P. Dočolomanský, V. Boháčová, and A. Breier

Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, SK-842 33 Bratislava


Abstract: The inhibitory effect of eight anthraquinone derivatives on the ATP hydrolytic activity of Na+, K+-ATPase from dog kidney was studied. The magnitude of the inhibitory action of these substances was found to depend on the apparent acid-base dissociation constant (pKa(app)). Namely, when the pKa(app) values exceeded the level 7.1, the inhibitory actions of the respective anthraquinones steeply decreased. Additionally, inhibitory effect of anthraquinones was found to be potentiated by the existence of triazine moiety in the molecule. The presence of the areas with ''high density of electrons'' in the anthraquinone molecule (e.g. the sulfoethylsulfonyl chain in the molecule of Remazol Brilliant Blue R) also potentiated their inhibitory action.

Full paper in Portable Document Format: 482a128.pdf


Chemical Papers 48 (2) 128–132 (1994)

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