Landon F, Huc C, Thomé F, Oriol C, Olomucki A
Eur J Biochem. 1977 Dec;81(3):571-7. doi: 10.1111/j.1432-1033.1977.tb11984.x.
Human blood platelet actin was purified using 30% sucrose to extract actomyosin and potassium iodide to dissociate actomyosin and to depolymerize actin. Pure actin thus obtained resembles skeletic muscle actin in its polymerization properties, CD spectra and ability to activate myosin myosin Mg2+-ATPase. Isoelectric focusing gel analysis shows that human blood platelet actin exists in beta and gamma forms. The ratio of beta to gamma forms is of 5 in purified actin, in whole cell extract and in all the fractions studied.
使用30%的蔗糖提取肌动球蛋白，并用碘化钾解离肌动球蛋白和解聚肌动蛋白，从而纯化人血小板肌动蛋白。如此获得的纯肌动蛋白在其聚合特性、圆二色光谱以及激活肌球蛋白Mg2 + -ATP酶的能力方面类似于骨骼肌肌动蛋白。等电聚焦凝胶分析表明，人血小板肌动蛋白以β和γ两种形式存在。在纯化的肌动蛋白、全细胞提取物以及所有研究的组分中，β形式与γ形式的比例均为5。
