Figure 2.

Analysis of HrpZ oligomer size on nondenaturing polyacrylamide gel with N‐perfluoro‐octanoic acid (PFO), a lipid mimic. The relative mobility (R_f) of a protein in the gel is inversely proportional to the logarithm of the molecular weight. The standard proteins (◆) used to determine the size of HrpZ_Pph native forms (□) were IgM (950 kDa), thyroglobulin (670 and 335 kDa), ferritin (440 kDa), myosin (210 kDa), β‐galactosidase (120 kDa), bovine serum albumin (85 kDa), ovalbumin (50 kDa), carbonic anhydrase (33 kDa) and soybean trypsin inhibitor (28.5 kDa). Myosin and the smaller standard proteins were covalently prestained. The inset shows the HrpZ_Pph profile on a PFO native gel blot, with arrows indicating the monomer and oligomer bands.