Actin co-purifies with RNA polymerase II.
Actin co-purifies with RNA polymerase II.
复制标题
肌动蛋白与 RNA 聚合酶 II 共同纯化。
DOI：
10.1016/0006-291x(79)90395-4
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发表时间：
1979
影响因子：
3.1
通讯作者：
B. Jockusch
中科院分区：
文献类型：
--
作者：
Steven S. Smith;Kristin H. Kelly;B. Jockusch
RNA聚合酶II，[EC2.7.7.6]，来自黏菌多头绒泡菌，纯化超过4000倍，可含有表观分子量为46，000的蛋白质。通过非变性条件下的聚丙烯酰胺凝胶电泳和磷酸纤维素层析，将该蛋白质与RNA聚合酶II的推定亚基分离。在这份报告中，我们确定的蛋白质肌动蛋白，我们指出，这种表观分子量的多肽已被发现与RNA聚合酶II从其他来源纯化也可能是肌动蛋白从这些生物体。
RNA polymerase II, [EC2.7.7.6], from the slime moldPhysarum polycephalum, purified over 4000-fold can contain a protein with an apparent molecular weight of 46,000. This protein is separated from the putative subunits of RNA polymerase II by polyacrylamide gel electrophoresis under non-denaturing conditions, and by chromatography on phosphocellulose. In this report we identify the protein as actin, and we point out that polypeptides of this apparent molecular weight which have been found associated with RNA polymerase II purified from other sources may also be actin from these organisms.