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
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Zusammenfassung:	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.
ISSN:	0014-4754 1420-9071
DOI:	10.1007/BF01942849