Craig R, Megerman J
J Cell Biol. 1977 Dec;75(3):990-6. doi: 10.1083/jcb.75.3.990.
The in vitro assembly of myosin purified from calf aorta muscle has been studied by electron microscopy. Two types of filament are formed: short bipolar filament similar to those formed from skeletal muscle myosin, and longer "side-polar" filaments having cross bridges with a single polarity along the entire length of one side and the opposite polarity along the other side. Unlike the case with skeletal myosin filaments, antiparallel interactions between myosin molecules occur along the whole length of side-polar filaments. The side-polar structure may be related to the in vivo form of myosin in vertebrate smooth muscle.
通过电子显微镜对从小牛主动脉肌肉中纯化的肌球蛋白进行了体外组装研究。形成了两种类型的细丝:类似于由骨骼肌肌球蛋白形成的短双极细丝,以及较长的“侧极”细丝,其沿一侧的整个长度具有单一极性的横桥,而沿另一侧具有相反的极性。与骨骼肌肌球蛋白细丝的情况不同,肌球蛋白分子之间的反平行相互作用沿着侧极细丝的整个长度发生。侧极结构可能与脊椎动物平滑肌中肌球蛋白的体内形式有关。