Dynamic characteristics of F-actin and thin filaments in vivo and in vitro.

F Oosawa, Y Maeda, S Fujime, S Ishiwata, T Yanagida, M Taniguchi
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Abstract

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.

f -肌动蛋白及细丝的体内外动态特性。
对溶液中的f -肌动蛋白和甘油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。在相同浓度下,肌原纤维i波段的双折射与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具有相同的数量级。i波段的紫外二色性与F-actin或F-actin复合物的紫外二色性非常相似,这是由于F-actin中结合的ADP和色氨酸残基的取向。准弹性光散射测量、电子显微镜观察和i波段电光效应分析表明,f -肌动蛋白在体外和体内的细丝具有大致相同的柔韧性。这些在不同条件下进行的光学测量为体内和体外钙离子诱导f -肌动蛋白的构象变化提供了证据。这种构象变化被发现被f -肌动蛋白与肌球蛋白的相互作用放大。本文就f -肌动蛋白及其细丝在体内和体外的光学研究进展作一综述。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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