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. Author manuscript; available in PMC: 2018 Jan 22.
Published in final edited form as: Biochem Biophys Res Commun. 2016 Dec 10;482(4):1437–1442. doi: 10.1016/j.bbrc.2016.12.054

Figure 1. SDS-polyacrylamide gel images from purification of recombinant retroviral Gag proteins.

Figure 1

(A) Western blotting of the lysates from induced E. coli expressing full-length GagBH10 (Lane 1) and GagΔp6BH10 (Lane 2). (B) Products from major steps of protein purification for HIV-1 GagΔp6BH10. Lanes: 1: protein marker; 2: total lysate of cell pellet after 5-hour induction; 3: supernatant from cell lysate after 0.2% PEI treatment; 4: re-dissolution of protein pellet after 33% ammonium phosphate precipitation; 5: elution fraction after PC resin purification; 6: final product after heparin column chromatography. (C–F) Purity tests for various versions of recombinant retroviral Gag proteins: GagΔp6BH10 (C); GagΔp6NL4-3 (D); Gag ΔMA Δp6BH10 (E); and RSV Gag ΔMBDΔPR (F). The amounts of protein loaded in each lane were 30 µg, 6 µg, 3 µg, and 1.5 µg for (C), (D) and (E), corresponding to 100%, 20%, 10% and 5% respectively. The amounts of protein loaded in each lane for (F) were 25 µg, 2.5 µg, 1.25 µg, and 0.5 µg, corresponding to 100%, 10%, 5% and 2% respectively.