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Interaction of Phalloidin with Actin

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Lengsfeld,  Anneliese
Max Planck Institute for Medical Research, Max Planck Society;

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Löw,  Irmentraut
Max Planck Institute for Medical Research, Max Planck Society;

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Wieland,  Theodor
Max Planck Institute for Medical Research, Max Planck Society;

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Dancker,  Peter
Max Planck Institute for Medical Research, Max Planck Society;

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Hasselbach,  Wilhelm
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Lengsfeld, A., Löw, I., Wieland, T., Dancker, P., & Hasselbach, W. (1974). Interaction of Phalloidin with Actin. Proceedings of the National Academy of Sciences of the United States of America, 71(7), 2803-2807. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/4368830.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-E265-C
Abstract
Phalloidin, a toxic bicyclic peptide of rapid action from the toadstool, Amanita phalloides, gives rise to polymerization of G-actin to filamentous structures (Ph-actin) in a medium of low ionic strength. Ph-actin closely resembles the microfilaments found in liver membrane fractions (Ph-filaments) after in vivo or in vitro poisoning. Both phalloidin induced filaments are resistant to 0.6 M KI in contrast to F-actin, and become decorated by heavy meromyosin. After preincubation with cytochalasin B significantly fewer actin filaments are observed.