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. 2009 Jan 28;15:241–249.

Figure 6.

Figure 6

Hetero-oligomerization of βB2 with βA3. βB2 was mixed with either βA3 WT (A) or βA3 DM (B) and mixtures were immediately subjected to SEC-MALS (bottom panel) or incubated at 37 °C (middle panel) or 55 °C (top panel) for 90 min as for βB1 in Figure 3. Molar masses of βB2:βA3 WT peaks indicated predominantly dimers at 37 °C with a slight shift in elution volume and oligomers at 55 °C. Molar masses of βB2:βA3 DM peaks indicated predominantly dimers at 37 °C without a shift in elution volume and no oligomers were detected at 55 °C. Differences in hetero-oligomer formation were confirmed by subjecting mixtures of βB2 with βA3 WT or βA3 DM incubated at 37 °C for 60 min to Blue-Native-PAGE (C). Proteins were βB2 (lane 1), βA3 WT (lane 2), βA3 DM (lane 3), βB2:βA3 WT (lane 4), and βB2:βA3 DM (lane 5). Arrows indicate migration position of proteins.