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. 2019 May 10;294(26):10131–10145. doi: 10.1074/jbc.RA119.008294

Figure 2.

Figure 2.

Characterization of hPAH and C29S. A, intrinsic fluorescence of WT hPAH and C29S in the absence or presence of activating concentrations of Phe. B, activation by Phe promotes oligomerization of C29S. Shown is a linearized plot of S.E. data from a single rotor speed (10,000 rpm) for 2.5 μm C29S in the absence (gray circles) and presence of 1 mm Phe (open circles) at 4 °C. The slopes are proportional to M̄w at the given value of r2. Shown as dashed lines are the calculated lines expected for a monomer, dimer, and tetramer, respectively. See Fig. S2 for global fits to three rotor speeds and two concentrations in each state. C, SEC profiles of C29S in the absence and presence of saturating Phe. Black arrows indicate the elution volume (Ve) for the following standard proteins: 1, blue dextran (2000 kDa); 2, ferritin (440 kDa); 3, catalase (232 kDa); 4, aldolase (158 kDa); 5, BSA (67 kDa); and 6, bovine serum ovalbumin (43 kDa).