Borovikov Y S, Karandashov E A
Biochem Int. 1983 Sep;7(3):319-28.
The polarized fluorescence of intrinsic tryptophan residues and the birefringence of ghost muscle fibres of rabbit were measured during thin filaments binding to heavy meromyosin containing 5,5'-dithiobis [2-nitrobenzoic acid] light chains and to those devoid of them with a view of investigating conformational changes in F-actin. Ca2+ binding to heavy meromyosin containing 5,5'-dithiobis [2-nitrobenzoic acid] light chains was shown to affect the character of these changes during the formation of the F-actin - heavy meromyosin complex.
为了研究F-肌动蛋白的构象变化，在细肌丝与含有5,5'-二硫代双[2-硝基苯甲酸]轻链的重酶解肌球蛋白以及不含该轻链的重酶解肌球蛋白结合的过程中，测量了兔肌纤维膜的固有色氨酸残基的偏振荧光和双折射。结果表明，在F-肌动蛋白-重酶解肌球蛋白复合物形成过程中，Ca2+与含有5,5'-二硫代双[2-硝基苯甲酸]轻链的重酶解肌球蛋白结合会影响这些变化的特征。
