The rate of MgADP binding to and dissociation from acto-S1

J. Borejdo, T. Ando, T. P. Burghardt

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


The rate of binding and dissociation of MgADP from its ternary complex with actin and S1 was measured by following the extent to which fixed concentrations of MgADP slow down MgATP-induced dissociation of acto-S1. The solution of the equations describing this process shows that at any MgADP concentration the apparent rate of acto-S1 dissociation should be proportional to a square root of the equilibrium constant for MgADP dissociation and to MgATP concentration. By measuring the apparent rate of acto-S1 dissociation as a function of MgATP concentration, the rate of MgADP binding and dissociation were determined as 5 · 106 M-1 · s-1 and 1400 s-1, respectively. These rates were unchanged by modification of SH1 thiol of S1 by a variety of fluorescence and spin-labels, but dissociation rate was drastically reduced when SH1 was labelled with 5-iodoacetamidofluorescein.

Original languageEnglish (US)
Pages (from-to)172-176
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
StatePublished - Apr 5 1985


  • (Rabbit skeletal muscle)
  • Actin-myosin interaction
  • Dissociation rate constant
  • Fluorescence probe
  • MgADP binding
  • Myosin subfragment 1

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology


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