Open AccessInteraction of Phalloidin with Actin
Author(s) -
Anneliese M. Lengsfeld,
Irmentraut Löw,
Theodor Wieland,
Peter Dancker,
Wilhelm Hasselbach
Publication year - 1974
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.7.2803
Subject(s) - phalloidin , heavy meromyosin , microfilament , amanita phalloides , actin , biophysics , cytochalasin b , chemistry , biochemistry , biology , cytoskeleton , in vitro , cell , botany
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) afterin vivo orin 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.