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Conference Paper

Interaction between palytoxin and purified Na, K-ATPase

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Grell,  Ernst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Lewitzki,  Erwin
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Grell, E., Lewitzki, E., & Uemura, D. (1988). Interaction between palytoxin and purified Na, K-ATPase. In J. A. Skou, & J. G. Nørby (Eds.), Progress in Clinical and Biological Research (pp. 393-400). New York: Alan R. Liss, Inc.


Cite as: https://hdl.handle.net/21.11116/0000-0008-A448-E
Abstract
Palytoxin represents a group of extremely toxic substances which can be isolated from several Palythoa species. These toxins exhibit fairly complex structures as shown in Fig. 1 for the simplest analogue. Atempts to study the molecular interactions reveal that it interacts with membranes, eg. by increasing alkali ion permeabilities in a way which seems to be linked to membrane proteins such as Na, K-ATPase. Even similarities between palytoxin and ouabain concerning its inhibitory action on Na, K-ATPase have been reported. In addition, as a fairly unexpected property of the toxin a promoting effect due to borate is indicated. Although lytoxin binds to membrane-bound Na, K-ATPase, no interactions have so far been studied on the purified enzyme