Purification of actin from cardiac muscle.
Purification of actin from cardiac muscle.
复制标题
从心肌中纯化肌动蛋白。
DOI：
10.1080/00327488108065530
复制
发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Potter,JD
中科院分区：
文献类型：
--
作者：
Zot,HG;Potter,JD
肌动蛋白从心脏丙酮和乙醚粉末相比，肌动蛋白从骨骼丙酮粉末使用修改的既定提取程序。从心脏乙醚粉末中得到的肌动蛋白的产率几乎与从骨骼丙酮粉末中得到的产率相同，而从心脏丙酮粉末中得到的肌动蛋白明显较少。十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示，从每个来源的肌动蛋白是几乎相同的纯度和流动性。G-肌动蛋白的分子筛层析证明来自乙醚粉末的心脏肌动蛋白具有与来自丙酮粉末的骨架肌动蛋白相同的聚合和流动性。一个简化的程序，开发高度纯化肌动蛋白从肌肉粉末和制备在一天之内。还讨论了F-肌动蛋白在-80 ℃下的贮存。
Actin from cardiac acetone and ether powders is compared to actin from skeletal acetone powder using a modification of an established extraction procedure. The yield of actin from cardiac ether powder is nearly the same as the yield from skeletal acetone powder whereas significantly less actin is obtained from cardiac acetone powder. Sodium dodecyl sulfate polyacrylamide gel electrophoresis shows the actins from each of the sources to be virtually identical in terms of purity and mobility. Molecular sieve chromatography of G-actin demonstrates cardiac actin from ether powder to have identical polymerization and mobility properties as skeletal actin from acetone powder. A simplified procedure, developed for highly purified actin from muscle powder and prepared in a single day is presented. The storage of F-actin at -80 C is also discussed.