Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers

Danuta Szczesna-Cordary, Yu S. Borovikov, N. N. Lebedeva, I. Kakol

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The binding of phosphorylated heavy meromyosin to regulated F-actin in ghost fibers at high Ca2+ concentration increases, and at low Ca2+ concentration decreases, the anisotropy of intrinsic tryptophan fluorescence of F-actin. The effect is opposite to the effect of the binding of dephosphorylated heavy meromyosin.

Original languageEnglish
Pages (from-to)194-196
Number of pages3
JournalExperientia
Volume43
Issue number2
DOIs
StatePublished - Feb 1 1987
Externally publishedYes

Fingerprint

Myosin Subfragments
Myosin Light Chains
Phosphorylation
Actins
Fibers
Anisotropy
Tryptophan
Fluorescence

Keywords

  • ghost muscle fiber
  • Phosphorylated heavy meromyosin
  • regulated F-actin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers. / Szczesna-Cordary, Danuta; Borovikov, Yu S.; Lebedeva, N. N.; Kakol, I.

In: Experientia, Vol. 43, No. 2, 01.02.1987, p. 194-196.

Research output: Contribution to journalArticle

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