Abstract
The two-dimensional gel electrophoresis has been used as a powerful tool to separate proteins, and it is recently used as good resolution method for the subsequent mass spectrometric analysis. Generally, pretreatment of samples for two-dimensional electrophoresis involves solubilization, denaturation and reduction to completely break up the interactions among proteins, and removal of all interfering compounds to ensure efficient separation. One of the problems in the pretreatment is that large amount of proteins is lost, because some proteins would be aggregate and difficult to resolubilize them. Here, we show the method to get reproducibly clear images of the two-dimensional gel electrophoresis without complicated pretreatment.