Oosawa F, Maeda Y, Fujime S, Ishiwata S, Yanagida T, Taniguchi M
J Mechanochem Cell Motil. 1977 Mar;4(1):63-78.
Measurements of birefringence, ultraviolet dichorism and quasielastic light scattering were carried out on F-actin in solution and on the thin filaments of glycerinated myofibrils. The birefringence of the I-bands of myofibrils was of the same order of magnitude as that of F-actin or the F-actin-tropomyosin-troponin complex oriented in vitro at the same concentration. The ultraviolet dichroism spectrum of the I-bands was very similar to that of F-actin or the F-actin complex in vitro, which is due to orientation of bound ADP and tryptophan residues in F-actin. Quasielastic light scattering measurements, electronmicroscopic observations and the analyses of the electro-optic effect of the I-bands suggested approximately the same flexibility for F-actin in vitro and for the thin filaments in vivo. These optical measurements which were made under various conditions provide evidence for a conformational change induced by calcium ions in F-actin both in vivo and in vitro. This conformational change was found to be amplified by the interaction of F-actin with myosin. This is a brief review of our investigation on the dynamics of F-actin and the thin filament in vivo and in vitro by optical methods.
对溶液中的F-肌动蛋白以及甘油处理的肌原纤维细丝进行了双折射、紫外二色性和准弹性光散射测量。肌原纤维I带的双折射与相同浓度下体外定向的F-肌动蛋白或F-肌动蛋白-原肌球蛋白-肌钙蛋白复合物的双折射处于同一数量级。I带的紫外二色性光谱与体外F-肌动蛋白或F-肌动蛋白复合物的光谱非常相似,这是由于F-肌动蛋白中结合的ADP和色氨酸残基的取向所致。准弹性光散射测量、电子显微镜观察以及I带的电光效应分析表明,体外的F-肌动蛋白和体内的细丝具有大致相同的柔韧性。在各种条件下进行的这些光学测量为钙离子在体内和体外诱导F-肌动蛋白构象变化提供了证据。发现这种构象变化通过F-肌动蛋白与肌球蛋白的相互作用而被放大。这是我们通过光学方法对体内和体外F-肌动蛋白和细丝动力学研究的简要综述。