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. 2011 Jul 18;6(7):e21889. doi: 10.1371/journal.pone.0021889

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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A- Purified GST, GST-tagged ATGL(1–366) or GST-tagged ATGL(300–504) was bound to glutathione Sepharose beads, then incubated with E. coli lysates expressing the His-tagged DCB domain of GBF1. Eluted proteins were analyzed by Western blotting using His antibody. B- and C- The indicated His-tagged GBF1 domain expressed in E. coli was bound to Ni Sepharose 6 Fast Flow, then purified GST or the indicated GST-tagged domain of ATGL were incubated with the protein-bound beads. Eluted proteins were analyzed by Western blotting using GST antibody. B- The HDS1-His domain of GBF1 bound to Ni Sepharose beads. C- The His-tagged Sec7 domain of GBF1 bound to Ni Sepharose beads.