Effects of tryptic digestion on myosin subfragment 1 and its actin-activated adenosinetriphosphatase.
Effects of tryptic digestion on myosin subfragment 1 and its actin-activated adenosinetriphosphatase.
复制标题
胰蛋白酶消化对肌球蛋白亚片段 1 及其肌动蛋白激活的腺苷三磷酸酶的影响。
DOI：
10.1021/bi00269a043
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Morales,MF
中科院分区：
文献类型：
--
作者：
Botts,J;Muhlrad,A;Takashi,R;Morales,MF
结果与其他人的报告一致[例如，Balint等人（1978）]，发现Sl的有限胰蛋白酶消化基本上产生三个重链片段（20K， 50K和27K），它们在低kc1溶液中仍然存在关联，但可以通过聚丙烯酰胺凝胶电泳分离。如图1所示，重链几乎完全降解为三个片段。TRFAD测量显示，已消化和未消化的标记Sl的$值没有显著差异，证实片段仍然存在关联（表1）。标记的Sl （0.25 fiM）与F-actin （1.0 juM）的相互作用使这两个$值增加到大约相同的程度，表明actin与切割和未切割的结合程度相当
ResultsIn agreement with reports by others [eg, Balint et al.(1978)], limited tryptic digestion of Sl was found to produce essentially three heavy chain fragments (20K, 50K, and 27K) which remain associated in lowKC1 solution but are separable by polyacrylamide gel electrophoresis. As shown in Figure1, the heavy chain is almost completely degraded into the three fragments.TRFAD measurements reveal no significant difference in the $ values for digested and undigested labeled Sl, con-firming that the fragments remain associated (Table I). Interaction of labeled Sl (0.25 fiM) with F-actin (1.0 juM) increased these two $ values to about the same degree, indicating an equivalent extent of actin binding to cut and uncut