Summary
3H-desmethylphalloin (DMPh), a phallotoxin chemically very similar to phalloidin, binds specifically to rat liver plasma membranes in vitro. Already after 30 sec at 37°C, >90% of maximal binding had taken place. At low 3H-DMPh concentrations, isolated plasma membranes bind 20 times more of the cyclopeptide per mg protein as compared with microsomes or mitochondria. Scatchard plot argues for the presence of two different binding sites in the plasma membranes. The dissociation constants of them at 37°C are 2.2·10−8 moles/l and 1.2·10−6 moles/l, respectively. 3H-DMPh bound on membranes could be exchanged by nonlabeled phalloidin but not by antamanide or tetraethylammonium ions.
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Lutz, F., Glossmann, H. & Frimmer, M. Binding of 3H-desmethylphalloin to isolated plasma membranes from rat liver. Naunyn-Schmiedeberg's Arch. Pharmacol. 273, 341–351 (1972). https://doi.org/10.1007/BF00499668
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DOI: https://doi.org/10.1007/BF00499668