Bordas J, Lowy J, Svensson A, Harries J E, Diakun G P, Gandy J, Miles C, Mant G R, Towns-Andrews E
Physics Department, Liverpool University, United Kingdom.
Biophys J. 1995 Apr;68(4 Suppl):99S-104S; discussion 104S-105S.
Using synchrotron radiation and whole muscles, 2 ms time-resolved x-ray diffraction patterns were recorded at 8 degrees C. The results show that in both isotonic and isometric contractions, as well as in length changes imposed at maximum tension [Po], the meridional third myosin layer line consists of two distinct reflections with different intensities and spacings that measure approximately 14,623 and 14,412 nm at Po. Although the intensity behavior of the two reflections is strikingly different during quick releases, it is very similar during stretches. Study of the time courses indicates that myosin heads diffracting at Po with the approximately 14.623 nm periodicity are actively involved in tension production. Those diffracting at Po with the periodicity of approximately 14.412 nm appear not be associated with tension production during isometric contraction and releases, but the results suggest that they are recruited during stretches and here contribute to tension production. Our most important conclusion is that under all conditions of contraction we have investigated there exist two populations of myosin heads, each with a well defined axial disposition and configuration.
利用同步辐射和完整肌肉,在8摄氏度下记录了2毫秒时间分辨的X射线衍射图谱。结果表明,在等张收缩和等长收缩以及在最大张力[Po]下施加的长度变化中,肌球蛋白的子午第三层线由两个具有不同强度和间距的不同反射组成,在Po时测量值约为14,623和14,412纳米。尽管在快速释放过程中这两个反射的强度行为明显不同,但在拉伸过程中非常相似。对时间进程的研究表明,在Po处衍射且具有约14.623纳米周期性的肌球蛋白头部积极参与张力产生。那些在Po处衍射且具有约14.412纳米周期性的肌球蛋白头部在等长收缩和释放过程中似乎与张力产生无关,但结果表明它们在拉伸过程中被募集并在此处有助于张力产生。我们最重要的结论是,在我们研究的所有收缩条件下,存在两种肌球蛋白头部群体,每个群体都有明确的轴向排列和构型。