Takagi T, Kubo K
Biochim Biophys Acta. 1979 May 23;578(1):68-75. doi: 10.1016/0005-2795(79)90114-4.
The effects of 8 M urea on the complexes formed between sodium dodecyl sulfate and protein polypeptide were found to be as follows: (1) The maximum amount of SDS bound is reduced by almost half, and the minimum equilibrium concentration of SDS necessary to reach saturation was nearly doubled; (2) The apparent content of alpha-helical structure deduced from CD measurement is reduced to only 50--70% of that in the presence of sodium dodecyl sulfate alone; (3) The effective size of the sodium dodecyl sulfate-protein polypeptide complex deduced from viscosity measurements is increased, but is still smaller than the effective size of the protein in 8 M urea alone.
发现8M尿素对十二烷基硫酸钠与蛋白质多肽形成的复合物有如下影响：（1）结合的SDS最大量减少了近一半，达到饱和所需的SDS最小平衡浓度几乎增加了一倍；（2）从圆二色性测量推断的α-螺旋结构的表观含量仅降至单独存在十二烷基硫酸钠时的50%-70%；（3）从粘度测量推断的十二烷基硫酸钠-蛋白质多肽复合物的有效尺寸增加，但仍小于仅在8M尿素中蛋白质的有效尺寸。
