Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin
Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin
复制标题
DTNB轻链对脊椎动物骨骼肌球蛋白与肌动蛋白相互作用的影响
作者：
S. Margossian;S. Lowey;B. Barshop
来自脊椎动物骨骼肌的肌球蛋白含有四种低分子量亚基，被认为在肌球蛋白的酶活性中发挥功能性作用1，2去除“碱性轻链”（21，000和17，000 g mol−1）导致ATP酶活性完全丧失，但“DTNB轻链”解离（18，000 g mol−1）使肌球蛋白的酶活性基本不受影响3 -6。由于需要苛刻的溶剂将碱性轻链与重链解离（顾名思义），因此尚不清楚活性损失主要与重链变性还是与轻链去除相关7。
MYOSIN from vertebrate skeletal muscles contains four low molecular weight subunits which are thought to play a functional role in the enzymic activity of myosin1,2 Removal of ‘alkali light chains’ (21,000 and 17,000 g mol−1) results in complete loss of ATPase activity, but dissociation of ‘DTNB light chain’ (18,000 g mol−1) leaves the enzymic activity of myosin essentially unaffected3–6. Since harsh solvents are required to dissociate alkali light chains from heavy chains (as the name implies), it is unclear whether the activity loss is related primarily to denaturation of the heavy chain or to removal of the light chain7.