Effect of phosphorylation of rabbit skeletal muscle myosin light chains on the nature of conformational changes of F-actin induced by heavy meromyosin

S. Borovikov Yu., I. Konkol, D. Szczesna

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The changes in F-actin conformation in myosin-free single ghost fiber induced by the binding of heavy meromyosin (HMM) with dephosphorylated or phosphorylated light chains-2 (LC2) have been studied by measuring intrinsic tryptophan polarized fluorescence of F-actin. It has been found that at low concentrations of Ca2+ (pCa ≥ 8), the binding of HMM with dephosphorylated LC2 to F-actin in ghost fibres increases, whereas the binding of HMM with phosphorylated LC2 decreases the anisotropy of polarized tryptophan fluorescence. The effect is reversed at high concentrations of Ca2+ (pCa = 5). It has been assumed that this effect of myosin light chain phosphorylation may be due to its influence on the type of myosin head binding to F-actin.

Original languageEnglish (US)
Pages (from-to)691-694
Number of pages4
JournalBiokhimiya
Volume51
Issue number4
StatePublished - Jan 1 1986
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

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