Spatial relationship between SH1 and the actin binding site on myosin subfragment‐1 surface
Spatial relationship between SH1 and the actin binding site on myosin subfragment‐1 surface
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SH1与肌球蛋白亚片段-1表面肌动蛋白结合位点的空间关系
DOI：
10.1016/0014-5793(84)80914-x
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发表时间：
1984
期刊：
影响因子：
3.5
通讯作者：
K. Sutoh
中科院分区：
文献类型：
--
作者：
Keiichi Yamamoto;T. Sekine;K. Sutoh
为了研究SH 1巯基与亚片段1表面肌动蛋白结合位点之间的空间关系，我们研究了SH 1巯基与亚片段1表面肌动蛋白的相互作用，其SH 1被生物素的碘乙酸衍生物标记并被亲和素覆盖。亚片段-1-亲和素复合物与F-肌动蛋白结合，其Mg ~（2+）ATP酶活性被肌动蛋白激活。考虑到生物素结合位点的大小和位置，我们的结果表明，SH 1与亚片段1表面的肌动蛋白结合位点至少相隔17-20 μ m。
To examine the spatial relationship between SH1thiol and actin binding site on subfragment-1 surface, we studied the interaction with actin of subfragment-1 whose SH1was labeled with an iodoacetate derivative of biotin and covered with avidin. Subfragment-1-avidin complex bound F-actin and its Mg2+ATPase activity was activated by actin. Considering the size and the location of biotin binding site on avidin, our results suggest that SH1is separated from the actin binding site on subfragment-1 surface by at least 17–20 Å.