Figure 5

Two-dimensional electrophoretic pattern of 20S proteasome subunits. Purified 20S proteasomes (70 μg) from each strain were separated using a non-linear IPG strip (pH 3–10) in the first dimension (left to right) followed by SDS-PAGE in a 12% polyacrylamide gel in the second dimension (top to bottom). The 2-D gels were stained with Coomassie Brilliant Blue R-250. All labeled spots were identified by MALDI-TOF-MS and database searching (Table 1). The arrows indicate the shifts of the α1- and α7-subunits derived from the rpt6-1 proteasome towards the acidic side of the gel.