Kinetics of actin depolymerization: influence of ions, temperature, age of F-actin, cytochalasin B and phalloidin

Biochim Biophys Acta. 1986 Oct 17;873(3):387-96. doi: 10.1016/0167-4838(86)90088-9.

Abstract

Actin, labelled with the fluorescent dye N-(3-pyrenyl)maleimide, was diluted below its critical concentration and depolymerization was followed by measuring the declining fluorescence intensity. The time courses of depolymerization were fitted to a sum of three exponentials. In most cases there was a fast initial phase followed by one or three slower ones. Increasing MgCl2 concentration slowed down depolymerization velocity, as did substitution of Tris-maleate buffer by phosphate buffer. Older F-actin preparations depolymerized more slowly than younger ones. Phalloidin strongly decreased depolymerization velocity even after sonication. In the presence of cytochalasin B depolymerization was more uniformly exponential than in the absence of cytochalasin B; overall depolymerization velocity was decreased by cytochalasin B. The results are discussed on the assumption that depolymerization kinetics reflect the length distribution of actin filaments during depolymerization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Binding Sites / drug effects
  • Biopolymers
  • Cytochalasin B / pharmacology*
  • Deoxyribonuclease I / metabolism
  • Kinetics
  • Models, Chemical
  • Oligopeptides / pharmacology*
  • Osmolar Concentration
  • Phalloidine / pharmacology*
  • Spectrometry, Fluorescence
  • Temperature

Substances

  • Actins
  • Biopolymers
  • Oligopeptides
  • Phalloidine
  • Cytochalasin B
  • Deoxyribonuclease I