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  Interaction of actin with phalloidin:: Polymerization and stabilization of F-actin

Dancker, P., Löw, I., Hasselbach, W., & Wieland, T. (1975). Interaction of actin with phalloidin: Polymerization and stabilization of F-actin. Biochimica et Biophysica Acta: BBA, 400(2), 407-414. doi:10.1016/0005-2795(75)90196-8.

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BBA-ProteinStructure_400_1975_407.pdf (Any fulltext), 449KB
 
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 Creators:
Dancker, Peter1, Author           
Löw, Irmentraut1, Author           
Hasselbach, Wilhelm2, Author           
Wieland, Theodor1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The cyclic peptide phalloidin, one of the toxic components of Amanita phalloides prevented the drop of viscosity of F-actin solutions after the addition of 0.6 M KI and inhibited the ATP splitting of F-actin during sonic vibration. The data concerning ATP splitting are consistent with the assumption (a) that only 1 out of every 3 actin units of the filaments needs to be combined with phalloidin in order to suppress the contribution of these 3 actins to the ATPase activity of the filament and (b) that all actin units of the filaments can combine with phalloidin with a very high affinity. Phalloidin did not only stabilize the actin-actin bonds in the F-actin structure but it also increased the rate of polymerization of G-actin to F-actin. The ability of F-actin to activate myosin ATPase was not affected by phalloidin. The tropomyosin-troponin complex did not prevent the stabilizing effect of phalloidin on the F-actin structure.

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Language(s): eng - English
 Dates: 1975-02-262003-01-271975-08-19
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2795(75)90196-8
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Title: Biochimica et Biophysica Acta : BBA
  Other : Biochimica et Biophysica Acta (BBA) - Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 400 (2) Sequence Number: - Start / End Page: 407 - 414 Identifier: Other: 1879-2642
CoNE: https://pure.mpg.de/cone/journals/resource/18792642