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. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Neurobiol Dis. 2011 Sep 10;45(3):831–838. doi: 10.1016/j.nbd.2011.08.031

Fig. 1.

Fig. 1

In vitro analyses of the A4VSOD1 protein fraction show the presence of higher order oligomers, including high levels of a tetrameric species, compared to WTSOD1. A. Coomassie blue stained SDS-PAGE of purified WTSOD1 (WT) and A4VSOD1 (A4V) . The WT and A4V have an electrophoretic mobility at ~25 kDa, the expected molecular weight of the fusion proteins. B. Analytical ultracentrifugation of (blue line) wildtype SOD1 and (red line) A4VSOD1 protein in PBS. Dimer peaks were seen in both fractions as expected for the native active form of the metalloenzyme. The A4VSOD1 fraction contained multimeric species most notably a relatively large peak at the tetramer position while the wildtype SOD1 fraction primarily contained dimer. C. AFM fluid scan and particle sizing (inset) reveal the presence of large oligomers in the A4VSOD1 protein fraction measuring 12.4 nm in diameter. D. AFM fluid scan and particle sizing (inset) show smaller dimer-sized structures present in the WTSOD1 fraction with diameters measuring 5.5 nm.