Contribution of cysteines C59 and C61 in the first transmembrane helix (TM1) to the stabilization of the ASIC1a complex by BMOE.

<p>A: ASIC1a oligomeric states, resolved by SDS-PAGE under reducing conditions and detected by anti-His-tag western blotting (same experimental procedure as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135191#pone.0135191.g003" target="_blank">Fig 3A</a>), of the His<sub>8</sub>-tagged forms of ASIC1a-ΔC<sub>Ct</sub> as control (Ctrl), and the cysteine substitution mutant G433C-ΔC<sub>Ct</sub> (433), G433C-C59V-ΔC<sub>Ct</sub> (433–59) or G433C-C59V-C61S-ΔC<sub>Ct</sub> (433-59-61). Numbers I to IV have the same meaning as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135191#pone.0135191.g003" target="_blank">Fig 3</a>. B: Relative intensities (mean ±SEM, n = 4) of each of the 4 bands (I to IV) for ASIC1a identified on SDS-PAGE from cells expressing ASIC1a-ΔC<sub>Ct</sub>, (C), G433C-ΔC<sub>Ct</sub> (433) G433C-C59V-ΔC<sub>Ct</sub> (433–59) and G433C-C59V-C61S-ΔC<sub>Ct</sub> (433-59-61). The average molecular weight estimated for the four bands I, II, III, IV are respectively 80±10, 160±6, 230±9 and 300±19 kDa (Mw±SD, n = 4) for the G433C-ΔC<sub>Ct</sub>, G433C-C59V-ΔC<sub>Ct</sub>, and G433C-C59V-C61S-ΔC<sub>Ct</sub> constructs. * denotes p<0.01</p>