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. 2012 Feb 24;287(16):13194–13205. doi: 10.1074/jbc.M112.339655

FIGURE 2.

FIGURE 2.

Oligomerization in Fe-Dph4. A, immunodetection of Dph4 purified from yeast. Purified protein was separated on SDS-PAGE and immunodetected by Western blotting using anti-His antibody. B, iron-specific staining of Dph4 purified from E. coli and yeast separated on native PAGE. C, Western blot of Fe-Dph4 and Zn-Dph4 separated on native-PAGE and immunodetected by anti-His antibody. Increasing amounts of protein (4–20 μg) were loaded as indicated. D, iron staining of Dph4(93–149) purified from E. coli separated on native PAGE. Oligomers are marked with arrows.