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. 2011 Nov 22;5(2):191–199. doi: 10.1242/dmm.008490

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© 2012. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License (http://creativecommons.org/licenses/by-nc-sa/3.0), which permits unrestricted non-commercial use, distribution and reproduction in any medium provided that the original work is properly cited and all further distributions of the work or adaptation are subject to the same Creative Commons License terms.

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Fig. 1. — Analysis of the protein complexes of the vacuolar proteome by native electrophoresis and second dimension SDS-PAGE. Yeast cells were inoculated at initial A₆₆₀ 0.1 in SC medium and cultured for 24 hours; vacuoles were isolated as indicated in the Methods, and 100 μg samples were analyzed by blue-native electrophoresis to resolve protein complexes followed by a second dimension SDS-PAGE and western blotting using monoclonal antibodies that recognize the V-ATPase subunits Vma1p (69 kDa; V₁), Vph1p (100 kDa; V₀) and 60-kDa Vma2p (60 kDa; V₁), and V5 epitope (46 kDa; Btn1p-V5). (A) Analysis performed in isolated vacuoles from a wild-type strain harboring the empty plasmid pRS426. (B) Vacuoles isolated from a wild-type strain harboring pmBTN1-V5.