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. 2015 Mar 2;290(17):10689–10702. doi: 10.1074/jbc.M115.637058

FIGURE 3.

FIGURE 3.

Oligomeric stability of isolated apoA-IV triple and quadruple proline mutants. For each protein, the sample was first isolated at 4 °C by SEC. Purified oligomeric species of ApoA-IV and proline mutants were incubated at 37 °C for the indicated time and reanalyzed by SEC. The ratio is calculated as the area under the desired species divided by the total area of regions 1–3. A–C, stability of the purified WT dimer when compared with the single proline mutants (A), the double proline mutants (B), and the triple and quadrupole proline mutants (C). D, stability of purified trimer showing the WT dimer for comparison. Note: WT trimer cannot be isolated. E–H, individual SEC UV absorbance traces showing the distribution of oligomeric species over time for WT (E), P117/P139A/P161A/P183A dimer (F), P117A/P139A/P161A trimer (G), and P117/P139A/P161A/P183A trimer (H). mAU, milliabsorbance units.