Binding of phosphorylated and dephosphorylated heavy meromyosin to F‐actin

FEBS Letters

Ka̧kol, Irena¹  Szczçsna, Danuta¹  Sobieszek, Apolinary¹ 

[1] Institute of Molecular Biology, Austrian Academy of Sciences, 5020 Salzburg, Austria and Nencki Institute of Experimental Biology, 02-093 Warszawa, Poland

关键词: Meromyosin;    Phosphorylation;    Dephosphorylation;    Actin binding;    (Skeletal muscle);   

DOI  :  10.1016/0014-5793(87)81332-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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⁺.

【 授权许可】

Unknown