Rao P F, Takagi T
Institute for Protein Research, Osaka University.
J Biochem. 1989 Sep;106(3):365-71. doi: 10.1093/oxfordjournals.jbchem.a122859.
A reassessment study was made on the viscosity behavior of SDS-protein polypeptide complexes, since information about the nature of the complexes is important in establishing the principles of SDS-polyacrylamide gel electrophoresis. Measurements were made under two conditions, i.e., in a buffer of low concentration, and in a buffer of high concentration (usually used in standard SDS-polyacrylamide gel electrophoresis). Results in the former case were not consistent with viscometric data previously reported and widely accepted [Reynolds, J.A. and Tanford, C. (1970) J. Biol. Chem. 245, 5161-5165], and indicated that the complexes did not behave as a series of pseudo-homopolymers under the former conditions. Results in the latter case indicated that the complexes behaved much more like homologous polymers, but their viscosity behavior can only be interpreted in terms of flexible chains rather than a series of rigid rods with a constant diameter and variable lengths depending on their molecular weights.
由于关于复合物性质的信息对于确立SDS-聚丙烯酰胺凝胶电泳的原理很重要，因此对SDS-蛋白质多肽复合物的粘度行为进行了重新评估研究。在两种条件下进行了测量，即在低浓度缓冲液中以及在高浓度缓冲液中（通常用于标准SDS-聚丙烯酰胺凝胶电泳）。前一种情况下的结果与先前报道并被广泛接受的粘度数据不一致[雷诺兹，J.A.和坦福德，C.（1970年）《生物化学杂志》245卷，5161-5165页]，表明在前者条件下复合物的行为不像一系列假均聚物。后一种情况下的结果表明复合物的行为更类似于同源聚合物，但其粘度行为只能用柔性链来解释，而不是用一系列具有恒定直径且长度随分子量变化的刚性棒来解释。
