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. 1998 Sep 29;95(20):11828–11833. doi: 10.1073/pnas.95.20.11828

Figure 5.

Figure 5

HPLC gel filtration analysis of the HLA-DR2/MBP peptide complex. Because empty MHC class II molecules have a tendency to aggregate, the purified HLA-DR2/MBP peptide complex was examined by gel filtration chromatography (Bio-Sil SEC 250 column; Bio-Rad). Ten micrograms of DR2/MBP peptide complex was injected at time 0; the mobile phase was PBS, pH 6.8, the flow rate 1 ml/min, and the total run time 15 min. IgM, IgG, BSA, and β-lactoglobulin (molecular masses of >900, 150, 66.2, and 18.4 kDa) were used as standards (marked by arrows). The HLA-DR2/MBP peptide complex eluted at a molecular mass slightly higher than that of BSA. There was no evidence for aggregation of the HLA-DR2/MBP peptide complex. Axes as in Fig. 3.