Arii Yusuke, Hatori Kuniyuki
Department of Bio-System Engineering, Graduate School of Science and Engineering, Yamagata University, Yonezawa 992-8510, Japan.
Biochem Biophys Res Commun. 2008 Jul 11;371(4):772-6. doi: 10.1016/j.bbrc.2008.04.135. Epub 2008 May 5.
Both the sliding velocity of fluorescently labeled actin filament and its persistence length as an index of the bending flexibility of the filament were examined in the motility assay as varying the pH values of the solution for preparing actin filaments. When the pH value was varied from 5.0 to 9.0 in the solution in which actin filaments were formed from the constituent monomers, the motile performance of Mg(2+) bound actin filaments (Mg-F-actin) was apparently suppressed compared to the case of Ca(2+) bound ones (Ca-F-actin). The persistence length for Ca-F-actin gradually increased with the increase of the pH value while the similar length for Mg-F-actin remained rather independent of the value. The largest sliding velocity of the filament, on the other hand, obtained at the persistence length of roughly 6 microm for both cases of Mg-F-actin and Ca-F-actin.
在运动性测定中,通过改变用于制备肌动蛋白丝的溶液的pH值,研究了荧光标记的肌动蛋白丝的滑动速度及其作为丝弯曲柔韧性指标的持续长度。当在由组成单体形成肌动蛋白丝的溶液中pH值从5.0变化到9.0时,与结合Ca(2+)的肌动蛋白丝(Ca-F-肌动蛋白)相比,结合Mg(2+)的肌动蛋白丝(Mg-F-肌动蛋白)的运动性能明显受到抑制。Ca-F-肌动蛋白的持续长度随着pH值的增加而逐渐增加,而Mg-F-肌动蛋白的类似长度则与该值相当独立。另一方面,对于Mg-F-肌动蛋白和Ca-F-肌动蛋白两种情况,在大约6微米的持续长度下获得了丝的最大滑动速度。