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

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 h...

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Veröffentlicht in:Experientia 1987-02, Vol.43 (2), p.194-196
Hauptverfasser: SZCZESNA, D, BOROVIKOV, Y. S, LEBEDEVA, N. N, KAKOL, I
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BOROVIKOV, Y. S
LEBEDEVA, N. N
KAKOL, I
description 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.
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subjects Actins - metabolism
Animals
Biological and medical sciences
Calcium - pharmacology
Cell physiology
F-actin
Fundamental and applied biological sciences. Psychology
ghost cells
Kinetics
meromyosin
Molecular and cellular biology
Muscle contraction
Muscles - metabolism
myosin
Myosin Subfragments - metabolism
Myosins - metabolism
Peptide Fragments - metabolism
Phosphorylation
Protein Binding
Rabbits
Spectrometry, Fluorescence
title Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers
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