Kensler R W, Woodhead J L
Department of Anatomy, School of Medicine, University of Puerto Rico, San Juan 00036-5067.
J Muscle Res Cell Motil. 1995 Feb;16(1):79-90. doi: 10.1007/BF00125312.
Although chicken myosin S1 has recently been crystallized and its structure analysed, the relaxed periodic arrangement of myosin heads on the chicken thick filament has not been determined. We report here that the cross-bridge array of chicken filaments is temperature sensitive, and the myosin heads become disordered at temperatures near 4 degrees C. At 25 degrees C, however, thick filaments from chicken pectoralis muscle can be isolated with a well ordered, near-helical, arrangement of cross-bridges as seen in negatively stained preparations. This periodicity is confirmed by optical diffraction and computed transforms of images of the filaments. These show a strong series of layer lines near the orders of a 43 nm near-helical periodicity as expected from X-ray diffraction. Both analysis of phases on the first layer line, and computer filtered images of the filaments, are consistent with a three-stranded arrangement of the myosin heads on the filament.
尽管鸡肌球蛋白S1最近已结晶并对其结构进行了分析,但鸡粗肌丝上肌球蛋白头部的松弛周期性排列尚未确定。我们在此报告,鸡肌丝的横桥阵列对温度敏感,在接近4摄氏度的温度下,肌球蛋白头部会变得无序。然而,在25摄氏度时,从鸡胸肌分离出的粗肌丝具有排列有序、近乎螺旋状的横桥排列,如在负染制剂中所见。这种周期性通过光学衍射和肌丝图像的计算变换得到证实。这些显示出一系列强烈的层线,接近预期的43纳米近螺旋周期性的级数,这是从X射线衍射得出的。对第一层线上相位的分析以及肌丝的计算机滤波图像均与肌球蛋白头部在肌丝上的三链排列一致。