Phalloidin reduces the release of inorganic phosphate during actin polymerization

Biochim Biophys Acta. 1990 Aug 17;1035(2):197-200. doi: 10.1016/0304-4165(90)90116-e.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / isolation & purification
  • Actins / metabolism*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Kinetics
  • Macromolecular Substances
  • Muscles / metabolism
  • Oligopeptides / pharmacology*
  • Phalloidine / pharmacology*
  • Phosphates / metabolism*
  • Rabbits

Substances

  • Actins
  • Macromolecular Substances
  • Oligopeptides
  • Phosphates
  • Phalloidine
  • Adenosine Triphosphate