Smith C W, Marston S B
FEBS Lett. 1985 May 6;184(1):115-9. doi: 10.1016/0014-5793(85)80665-7.
The Ca2+-sensitive thin filaments of aorta smooth muscle have been, disassembled into their constituent proteins, actin, tropomyosin and a 120-kDa protein. The 120-kDa protein bound to aorta actin-tropomyosin and inhibited its ability to activate myosin MgATPase. This inhibition correlated with the binding of one 120-kDa protein molecule per 29 actin monomers. Upon the addition of calmodulin to the actin-tropomyosin-120-kDa protein complex, the inhibition was relieved in 10(-4) M Ca2+ but not 10(-9) M Ca2+. The full release of inhibition was not accompanied by a full release of 120-kDa protein binding to actin-tropomyosin. A fully active, Ca2+-sensitive aorta thin filament has thus been reconstituted from just four components: actin, tropomyosin, 120-kDa protein and calmodulin.
主动脉平滑肌中对钙离子敏感的细肌丝已被分解为其组成蛋白,即肌动蛋白、原肌球蛋白和一种120 kDa的蛋白质。这种120 kDa的蛋白质与主动脉肌动蛋白 - 原肌球蛋白结合,并抑制其激活肌球蛋白MgATP酶的能力。这种抑制作用与每29个肌动蛋白单体结合一个120 kDa蛋白质分子相关。向肌动蛋白 - 原肌球蛋白 - 120 kDa蛋白质复合物中添加钙调蛋白后,在10⁻⁴ M钙离子存在下抑制作用得到缓解,但在10⁻⁹ M钙离子存在下则没有。抑制作用的完全解除并不伴随着120 kDa蛋白质与肌动蛋白 - 原肌球蛋白结合的完全释放。因此,仅由肌动蛋白、原肌球蛋白、120 kDa蛋白质和钙调蛋白这四种成分就重新构建出了一种完全活跃、对钙离子敏感的主动脉细肌丝。