Borovikov Iu S, Lebedeva N N
Tsitologiia. 1987 Oct;29(10):1192-5.
Dependence between the amplitude of tension, developed by glycerinated muscle fibers during rigidity, and the character of structural changes in F-actin, induced by the formation of actomyosin complex, was studied by polarized microfluorimetry and tensiometry. It is shown that during rigidity the anisotropy of intrinsic tryptophan residues as well as of rhodamine phalloidin bound to F-actin, and amplitude of tension depend on pH (6-8) and ionic strength (mu = 0.07 M-0.14 M) of solution. Greater changes in polarized fluorescence and in amplitude of tension were registered during rigidity in solutions with low ionic strength (mu = 0.07 M) and pH 8. It suggested that the amplitude of muscle fibre tension depends on the relative quantity of actin monomers, being in the "switched on" state.
通过偏振显微荧光测定法和张力测定法，研究了甘油处理的肌纤维在强直状态下产生的张力幅度与由肌动球蛋白复合物形成所诱导的F-肌动蛋白结构变化特征之间的相关性。结果表明，在强直状态下，内在色氨酸残基以及与F-肌动蛋白结合的罗丹明鬼笔环肽的各向异性和张力幅度取决于溶液的pH值（6 - 8）和离子强度（μ = 0.07 M - 0.14 M）。在低离子强度（μ = 0.07 M）和pH 8的溶液中，强直状态下偏振荧光和张力幅度的变化更大。这表明肌肉纤维张力幅度取决于处于“开启”状态的肌动蛋白单体的相对数量。
