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. 2006 Jan 2;172(1):55–66. doi: 10.1083/jcb.200510016

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Figure 3. — Sro7p binds directly to Sec4p. (A) Sro7p was purified from yeast using a multistep purification protocol (see Materials and methods). 1 and 1.8 μg of purified Sro7p were subjected to SDS-PAGE analysis and stained with Coomassie. (B) 4 μM GTPγS-, GDP-bound, or nucleotide-free (NF) GST-Sec4 (Sec4) or GST alone in the presence of GTPγS on glutathione beads were incubated with 1 μM of purified Sro7p at 4°C. The beads were pelleted, and bound Sro7p was detected by Western blot analysis with an Sro7p-specific (α-Sro7) antibody. Coomassie staining of the GST fusion proteins as used in this assay is shown as a loading control. The input represents 10% of total Sro7p.