调节性轻链影响由肌动蛋白诱导的肌球蛋白头部的改变。
Regulatory light chain influences alterations of myosin head induced by actin.
作者信息
Babiychuk E B, Stepkowski D, Danilova V M, Kakol I
机构信息
Research Institute of Physiology, Kiev State University, USSR.
出版信息
FEBS Lett. 1991 Dec 16;295(1-3):55-8. doi: 10.1016/0014-5793(91)81383-j.
The effect of magnesium-for-calcium exchange and phosphorylation of regulatory light chain (LC2) on structural organization of rabbit skeletal myosin head was studied by limited tryptic digestion. In the presence of actin, exchange of magnesium bound to LC2 by calcium in dephosphorylated myosin accelerates the digestion of myosin and heavy meromyosin heavy chain and increases the accumulation of a 50 kDa fragment. This effect is significantly diminished in the case of phosphorylated myosin. Thus, both phosphorylation and cation exchange influences the effect of actin binding on the structural organization of myosin head.
通过有限胰蛋白酶消化研究了镁钙交换和调节性轻链（LC2）磷酸化对兔骨骼肌肌球蛋白头部结构组织的影响。在肌动蛋白存在的情况下，去磷酸化肌球蛋白中钙与结合在LC2上的镁进行交换，加速了肌球蛋白和重酶解肌球蛋白重链的消化，并增加了50 kDa片段的积累。在磷酸化肌球蛋白的情况下，这种作用显著减弱。因此，磷酸化和阳离子交换都影响肌动蛋白结合对肌球蛋白头部结构组织的作用。
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