Toylor D L
J Cell Biol. 1976 Mar;68(3):497-511. doi: 10.1083/jcb.68.3.497.
The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin.
采用定量偏振光技术研究了单个经曲通提取的兔腰大肌纤维从僵直到松弛转变过程中的双折射变化。僵直状态下静息长度纤维的总双折射为(1.46±0.08)×10⁻³,Mg-ATP松弛后增加到(1.67±0.05)×10⁻³。焦磷酸松弛仅使总双折射略有增加,而随后的Mg-ATP松弛引起双折射的最大增加。晶格间距的变化不能解释松弛过程中双折射的总体增加。此外,总双折射的增加归因于固有双折射和形态双折射的增加。肌球蛋白提取后暴露于松弛溶液中时,双折射没有变化。制备了合成肌球蛋白丝并用松弛和僵直溶液处理。用僵直溶液处理的经负染的丝在两端有明显的不规则突起,而用松弛溶液处理的丝更呈纺锤形。这些结果与以下观点一致,即肌球蛋白的亚片段-2部分从肌球蛋白聚集体(轻酶解肌球蛋白)处向外倾斜,以使亚片段-1部分能够附着于肌动蛋白。