Cavadore J C, Axelrud-Cavadore C, Berta P, Harricane M C, Haiech J
Biochem J. 1985 Jun 1;228(2):433-41. doi: 10.1042/bj2280433.
A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin.
通过一种独创的方法，从牛主动脉中纯化出一种具有功能的血管平滑肌肌动蛋白，且该蛋白能够聚合。主动脉肌动蛋白由两种主要异构体和至少两种次要异构体组成。这种肌动蛋白既不能被环磷酸腺苷依赖性蛋白激酶也不能被C激酶磷酸化。除了氨基酸组成（含三个色氨酸残基而非四个）外，发现主动脉肌动蛋白的物理性质与骨骼肌肌动蛋白非常相似。主动脉肌动蛋白和骨骼肌肌动蛋白在骨骼肌肌球蛋白的镁离子依赖性ATP酶激活程度上存在差异。
