Brassard E, Turmel C, Noolandi J
Xerox Research Centre of Canada, Mississauga, Ontario.
Electrophoresis. 1991 May;12(5):373-5. doi: 10.1002/elps.1150120509.
Polyacrylamide gel electrophoresis (PAGE) of proteins denatured with SDS (sodium dodecyl sulfate) has been used successfully to separate proteins according to their molecular mass. In spite of the extensive use of this technique, the motion of the protein-SDS complex in a polyacrylamide gel is still not understood. Here we report on the observation of the orientation (in the field direction) and relaxation of protein-SDS complexes during pulsed intermittent field PAGE experiments. The results give an indication of the stiffness of the molecules and may be useful for the development of a technique to improve the separation of large proteins using pulsed electric fields.
用十二烷基硫酸钠（SDS）变性的蛋白质进行聚丙烯酰胺凝胶电泳（PAGE）已成功用于根据蛋白质的分子量分离蛋白质。尽管该技术得到了广泛应用，但蛋白质-SDS复合物在聚丙烯酰胺凝胶中的移动情况仍未完全明了。在此，我们报告在脉冲间歇电场PAGE实验中对蛋白质-SDS复合物的取向（沿电场方向）和弛豫的观察结果。这些结果表明了分子的刚性，可能有助于开发一种利用脉冲电场改进大蛋白质分离的技术。
