Physical characterization of myosin light chains.
Physical characterization of myosin light chains.
复制标题
肌球蛋白轻链的物理表征。
DOI：
10.1021/bi00597a008
复制
发表时间：
1978
期刊：
影响因子：
2.9
通讯作者：
A. Szent
中科院分区：
文献类型：
--
作者：
W. Stafford;A. Szent
本文报道了对几种动物肌球蛋白低分子量亚基（轻链）的大小和形状的研究结果。流体动力学、分析凝胶过滤和荧光各向异性衰减测量表明，这些轻链可以由具有约100 +/- A的最长轴的一般椭圆体模型表示。通过研究pH、离子强度、温度和盐酸胍对其圆二色性光谱的影响，对扇贝调节轻链的内部结构稳定性进行了研究。圆二色性光谱对pH值、离子强度和4 ~ 70 ℃的温度变化几乎完全不敏感，这表明该亚基含有非常稳定的结构区域，当它与肌球蛋白结合时，可能存在这种结构。
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.