title: Phalloidin reduces the release of inorganic phosphate during actin polymerization.
abstract: Phalloidin, an actin-filament stabilizing peptide from Amanita phalloides, did not inhibit ATP hydrolysis during actin polymerization but strongly retarded the release of the hydrolysis product Pi. Thus, the lifetime of the intermediate F-actin-ADP-Pi is significantly increased by phalloidin. The results suggest a close correlation between filament stability and F-actin-ADP-Pi intermediates.
authors.affiliation: Institut für Zoologie, Technische Hochschule Darmstadt, F.R.G.
authors.forename: P
authors.initials: P
authors.lastname: Dancker
authors.forename: L
authors.initials: L
authors.lastname: Hess
mesh_terms: D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000378:metabolism; D009842:Oligopeptides / Q000494:pharmacology*; D010590:Phalloidine / Q000494:pharmacology*; D010710:Phosphates / Q000378:metabolism*; D011817:Rabbits
chemical_list: D000199:Actins; D046911:Macromolecular Substances; D009842:Oligopeptides; D010710:Phosphates; D010590:Phalloidine; D000255:Adenosine Triphosphate