Prefractionation of intact proteins by reversed-phase and anion-exchange chromatography for the differential proteomic analysis of Saccharomyces cerevisiae.

The need for multidimensional separations for bottom-up proteomic analyses has been well demonstrated by many over the past decade. The vast majority of reported approaches has focused primarily on improving the separation once the sample has already been digested. The work presented in this study shows an improvement in multidimensional approaches by prefractionation of intact proteins prior to digestion and separation of the peptides.