Szczesna D, Sobieszek A, Kakol I
FEBS Lett. 1987 Jan 5;210(2):177-80. doi: 10.1016/0014-5793(87)81332-7.
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+.
在无ATP的情况下，研究了骨骼肌中肌球蛋白轻链磷酸化对磷酸化和去磷酸化重酶解肌球蛋白（HMM）与F-肌动蛋白结合亲和力的影响。对于磷酸化的HMM，在存在Ca2+时的亲和力比不存在时弱2.5倍（HMM二价结合位点仅用Mg饱和）。对于去磷酸化的HMM，情况相反，在存在Ca2+时结合力高2.4倍。
