Fig. 2.
Fig. 2. Purified α and β dimerization site peptides. A 10% Laemmli SDS gel stained with Coomassie Brilliant Blue is shown. The GST fusion proteins (2 μg/lane) are as follows: lanes 1 through 3, α18-21, α18-211857, and α18-211857-Δ46, respectively. Recombinant peptides after protease cleavage, rechromatography on glutathione-Sepharose, and preparative HPLC gel filtration are as follows: lanes 4 through 7, α18-21, α18-211857, α18-211857-Δ46, and β1-4+.

Purified α and β dimerization site peptides. A 10% Laemmli SDS gel stained with Coomassie Brilliant Blue is shown. The GST fusion proteins (2 μg/lane) are as follows: lanes 1 through 3, α18-21, α18-211857, and α18-211857-Δ46, respectively. Recombinant peptides after protease cleavage, rechromatography on glutathione-Sepharose, and preparative HPLC gel filtration are as follows: lanes 4 through 7, α18-21, α18-211857, α18-211857-Δ46, and β1-4+.

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