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Fig. 7. Coomassie Blue-stained 4-15% SDS-polyacrylamide gels demonstrate changes in synemin sedimentation properties when allowed to copolymerize with vimentin or GFAP (A) or to bind to vimentin or GFAP IFs (B). Numbers indicate molecular mass in kDa. (A) Mixtures of 
-synemin and buffer, or of -synemin and either vimentin or GFAP were assembled in 8 M urea buffer and dialyzed under conditions that promote the assembly of vimentin and GFAP IFs. After dialysis, the mixtures were ultracentrifuged and proteins in the supernatant (SN) and pellet (P) were analyzed by SDS-PAGE. Most -synemin was recovered in the supernatant in the absence of vimentin or GFAP, but was mostly in the pellet in the presence of these proteins. (B) -synemin was added either to vimentin or GFAP IFs or to polymerization buffer. After a 1-hour incubation, the mixtures were ultracentrifuged, and proteins in the supernatant (SN) and pellet (P) were analyzed by SDS-PAGE. In the presence of vimentin IFs, -synemin was mostly recovered in the supernatant. By contrast, in the presence of GFAP IFs, most -synemin was recovered in the pellet.
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