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. 2010 Sep 16;62(2):497–508. doi: 10.1093/jxb/erq283

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© 2010 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 6. — Yeast VDAC1p copurifies with 6×His-AtTSPO. The expressed 6×His-AtTSPO in yeast was solubilized from total microsomes and affinity purified using a Ni-NTA matrice, with microsomes from the yeast strain transformed with the empty vector (EV) used as control. (A) The input (IN), flowthrough (FT), the three successive washes (respectively W1, W2, and W3) and the elution fraction (E) were analysed by immunoblotting for the presence of AtTSPO, with VDAC1p and Gas1p as control membrane proteins. (B) The elution from 6×His-AtTSPO strain (lane 2) or the empty vector strain (lane 3) were separated by SDS-PAGE alongside M_r markers (lane 1); after blue colloidal staining of the polypeptides the main bands in lane 2 (arrowheads) were excised and in-gel tryptic-digested and the resulting peptides analysed by MALDI TOF/TOF; the identified peptide for each polypeptide are shown on the right with their start and end in the primary sequence of the MS/MS identified protein.