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. 2010 Aug 17;12(2):151–166. doi: 10.1111/j.1364-3703.2010.00655.x

Figure 7.

Figure 7

The C‐terminal deletion mutants were defective in oligomer formation. Left: immunoblot of the full‐length HrpZPph (WT) and HrpZPph deletion mutants ZΔA–ZΔJ (A–J), run on 5.5%–8% native polyacrylamide gel electrophoresis (PAGE) with N‐perfluoro‐octanoic acid (PFO). The samples were not heated before loading. Middle: the accumulation of dimers of the mutants ZΔI, ZΔA and ZΔB was reduced when the protein samples were heated at 65 °C in sample buffer containing 100 mm dithiothreitol (final concentration) before loading onto the gel. The full‐length protein (WT) was treated similarly to the mutants. Right: immunoblot of mutant Zm run on 6%–12% native PAGE with PFO. Note that this panel is not in the same scale as the two other panels; the molecular weight of Zm is only 21.1 kDa. m, monomer of HrpZ; d, dimer of HrpZ; o, large oligomer of HrpZ.