Andries C, Clauwaert J
Biophys J. 1985 May;47(5):591-605. doi: 10.1016/S0006-3495(85)83955-2.
The bovine eye lens protein, alpha L crystallin, has been studied with photon correlation spectroscopy and statical light scattering in the concentration range up to 200 g/l in different solvent conditions. At higher concentration (c greater than 70 g/l) the scattering behavior is quite complicated, which results in nonexponential correlation functions. Three methods have been used for the analysis of these correlation functions, namely, cumulant analysis, sum of two exponentials analysis, and exponential sampling method. These methods resulted in very similar results. The highly concentrated solutions contain two scattering entities: the single alpha L crystallin and a rather heterogeneous population of large clusters. The statical light-scattering experiments can be interpreted in the same way and gave consistent results for the dimensions of the large scattering units. The formation of these clusters, which are strong light scatterers, is superimposed on an increasing degree of correlation between the bulk of the alpha L-crystallins, resulting in a net decrease of light scattering as a function of concentration.
利用光子相关光谱法和静态光散射法,在不同溶剂条件下,对浓度高达200 g/l范围内的牛眼晶状体蛋白αL-晶体蛋白进行了研究。在较高浓度(c大于70 g/l)时,散射行为相当复杂,这导致相关函数呈非指数形式。已使用三种方法分析这些相关函数,即累积量分析、两个指数之和分析和指数抽样法。这些方法得出了非常相似的结果。高浓度溶液包含两个散射实体:单个αL-晶体蛋白和相当不均匀的大聚集体群体。静态光散射实验可以用相同的方式解释,并且对于大散射单元的尺寸给出了一致的结果。这些作为强光散射体的聚集体的形成,叠加在大部分αL-晶体蛋白之间不断增加的相关性程度上,导致光散射随浓度的净减少。