Stafford W F, Szent-Györgyi A G
Biochemistry. 1978 Feb 21;17(4):607-14. doi: 10.1021/bi00597a008.
This paper reports the results of an investigation into the size and shape of the low molecular weight subunits (light chains) of myosin from several animal species. Hydrodynamic, analytical gel filtration, and fluorescence anisotropy decay measurements indicated that these light chains could be represented by a general ellipsoidal model having a longest axis of about 100 +/- A. Investigation into the stability of the internal structure of the scallop regulatory light chain was carried out by studying the effect of pH, ionic strength, temperature, and guanidine hydrochloride on its circular dichroic spectrum. The nearly complete insensitivity of the circular dichroic spectrum to pH, ionic strength, and temperature variations from 4 to 70 degrees C indicated that this subunit contained regions of very stable structure which probably exist when it is bound to myosin.
本文报道了对几种动物物种肌球蛋白低分子量亚基（轻链）的大小和形状进行研究的结果。流体动力学、分析凝胶过滤和荧光各向异性衰减测量表明，这些轻链可以用一个长轴约为100±埃的一般椭球体模型来表示。通过研究pH值、离子强度、温度和盐酸胍对扇贝调节轻链圆二色光谱的影响，对其内部结构的稳定性进行了研究。圆二色光谱对pH值、离子强度以及4至70摄氏度温度变化几乎完全不敏感，这表明该亚基包含非常稳定的结构区域，这些区域可能在其与肌球蛋白结合时存在。
