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. 2013 May 15;24(10):1507–1518. doi: 10.1091/mbc.E13-01-0006

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© 2013 Mbantenkhu et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 4: — Chromatographic profile, oligomeric state and in vivo stability of mutant Mgm101. (A) Size exclusion chromatography of purified MBP-Mgm101 and its mutant variants on a calibrated Superose 6 column. V0, void volume. (B) Size exclusion chromatography of purified Mgm101 and its C-tail variants. (C) Size exclusion chromatography of Mgm101^W257A on a Superose 6 column before and immediately after the release from MBP (red line). Inset shows SDS–PAGE analysis of peaks 1 and 2, which contain MBP and Mgm101, respectively. (D) Western blot analysis showing the levels of the mutant Mgm101 in isolated mitochondria. The mitochondrial outer membrane protein porin is used as a control for calibrating sample loading.

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