13024_2016_145_MOESM2_ESM.pdf (505.92 kB)
Additional file 2: Figure S1. of Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis
journal contribution
posted on 2017-01-05, 05:00 authored by Eiichi Tokuda, Itsuki Anzai, Takao Nomura, Keisuke Toichi, Masahiko Watanabe, Shinji Ohara, Seiji Watanabe, Koji Yamanaka, Yuta Morisaki, Hidemi Misawa, Yoshiaki FurukawaPreparation of soluble disulfide-crosslinked SOD1 oligomers in vitro. E,E-SOD1S-S (100 μM) was incubated in the NNE buffer at 37 °C for five days and then centrifuged at 20,000 x g for 10 min. to remove any insoluble materials. The samples were further reacted with 100 mM iodoacetamide in the presence of 2% SDS and analyzed by (left) non-reducing and (right) reducing SDS-PAGE. The electrophoretic mobility of monomeric SOD1(G85R) has been known to be faster than those of the other SOD1 proteins (WT, A4V, and G37R). (PDF 505 kb)
