Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin

Danuta Szczçsna, Apolinary Sobieszek, Irena Ka̧kol

Research output: Contribution to journalArticle

8 Scopus citations


The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca2+ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca2+.

Original languageEnglish (US)
Pages (from-to)177-180
Number of pages4
JournalFEBS letters
Issue number2
StatePublished - Jan 5 1987



  • (Skeletal muscle)
  • Actin binding
  • Dephosphorylation
  • Meromyosin
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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