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. 2015 Aug 6;10(8):e0135031. doi: 10.1371/journal.pone.0135031

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© 2015 Furukawa et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 2 — Precocene II-binding protein was purified by using precocene II-immobilized magnetic beads with protein extracts from the mitochondria fraction (A), nuclear/unbroken cell fraction (B), and cytosolic fraction (C) of F. graminearum protoplasts, as well as from the mitochondria fraction of S. cerevisiae (E). Each protein extract was incubated with the beads, which were collected, washed three times with buffer, and eluted with a solution containing free precocene II. Pre II elution (−), third washing fraction; Pre II elution (+), free precocene II eluting fraction; Pre II competition, precocene II was added to protein extract before incubation with the beads. Separated proteins were visualized by silver staining. (D) Experiment with recombinant His-VDAC. Purified recombinant His-VDAC was incubated with precocene II-immobilized or control beads. Bead-bound proteins were eluted by boiling. His-VDAC was detected with anti-His antibody. FT, flow-through fraction (bead-unbound proteins).