Miyahara M, Noda H
J Biochem. 1979 Jul;86(1):239-48.
The electric dipole moment of rabbit skeletal myosin was estimated from the electric and flow birefringence properties. Myosin formed small polydisperse aggregates (0.2-1.1 microM in length) with an apparent electric dipole moment of 5,000-20,000 Debye in aqueous urea or sodium pyrophosphate at low ionic strength. Permanent dipole moment contributed substantially to the apparent dipole moment. An anti-parallel association of myosin was suggested from the dependence of the apparent dipole moment on myosin concentration. Some interactions between myosin and C-protein were detected in 1 M urea by flow birefringence and analytical ultracentrifugation studies. The apparent dipole moment of myosin aggregates was less dependent on myosin concentration in the presence of C-protein.
通过电双折射和流动双折射特性估算了兔骨骼肌肌球蛋白的电偶极矩。在低离子强度的尿素水溶液或焦磷酸钠中，肌球蛋白形成了小的多分散聚集体（长度为0.2 - 1.1微摩尔），其表观电偶极矩为5000 - 20000德拜。永久偶极矩对表观偶极矩有很大贡献。从表观偶极矩对肌球蛋白浓度的依赖性推测出肌球蛋白存在反平行缔合。通过流动双折射和分析超速离心研究在1 M尿素中检测到了肌球蛋白与C蛋白之间的一些相互作用。在存在C蛋白的情况下，肌球蛋白聚集体的表观偶极矩对肌球蛋白浓度的依赖性较小。
