title: Dynamic characteristics of F-actin and thin filaments in vivo and in vitro.
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.
mesh_terms: D000199:Actins / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001001:Anura; D001718:Birefringence; D002118:Calcium / Q000494:pharmacology; D003593:Cytoplasm / Q000502:physiology; D003599:Cytoskeleton / Q000502:physiology; D008027:Light; D009210:Myofibrils / Q000502:physiology; D009218:Myosins / Q000494:pharmacology; D011487:Protein Conformation; D012542:Scattering, Radiation; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins; D002118:Calcium