Coué M, Landon F, Olomucki A
Biochimie. 1982 Mar;64(3):219-26. doi: 10.1016/s0300-9084(82)80472-0.
A new procedure of purification of actin from human blood platelets was used. This method starting from acetone powder of whole platelets gives a much higher yield than the one previously described (actin I) (Landon et al. (1977) Eur. J. Biochem., 81, 571-577). This actin II preparation has the same reduced viscosity as skeletal muscle actin, while the reduced viscosity of actin I preparation is about 1/10 of this value. Moreover actin I has the form of very short filaments as shown by electron microscopy. After an extra step of purification actin I, when polymerized, acquired a high reduced viscosity. We confirmed that platelet and sarcomeric actins are similar in their polymerization properties and their ability to activate muscular myosin. A circular dichroism study showed that the overall conformation of both actins are similar, but the environment of their aromatic chromophores is different.
采用了一种从人血血小板中纯化肌动蛋白的新方法。这种从全血小板丙酮粉开始的方法，其产量比之前描述的方法（肌动蛋白I）（Landon等人，（1977年）《欧洲生物化学杂志》，81卷，571 - 577页）高得多。这种肌动蛋白II制剂的比浓粘度与骨骼肌肌动蛋白相同，而肌动蛋白I制剂的比浓粘度约为此值的1/10。此外，如电子显微镜所示，肌动蛋白I呈非常短的细丝形式。经过额外一步纯化后，肌动蛋白I聚合时获得了较高的比浓粘度。我们证实血小板肌动蛋白和肌节肌动蛋白在聚合特性和激活肌肉肌球蛋白的能力方面相似。圆二色性研究表明，两种肌动蛋白的整体构象相似，但它们芳香发色团的环境不同。
