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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: Protein Expr Purif. 2011 Jul 14;80(1):8–16. doi: 10.1016/j.pep.2011.06.013

Fig. 1.

Fig. 1

(A) Alignment of E6 sequences (upper half E6-N and lower half E6-C) from the BPV1 and several HPV species. Residues are numbered as in the shorter transcript of HPV 16 E6 (151 residues). Positions exhibiting conserved physicochemical characteristics are colored as follows: magenta, hydrophobic (W, F, Y, L, I, V, M); green, basic (K, R, H); red, acidic (E, D); orange, polar (Q, N, T, S); brown, cystein (C); cyan, small (G, A, P). (B) 15% SDS-PAGE gel showing the different purifications steps of BPV1 E6. Affinity-purified MBP-E6 was cleared from soluble aggregates by ultracentrifugation and digested using TEV protease. Subsequently, the sample was concentrated and injected on a HighLoad Superdex75 16/60 column. Lane 1: total cell lysate; lane 2: eluate from amylose resin before overnight ultracentrifugation; lane 3: eluate from amylose resin after overnight ultracentrifugation; lane 4: TEV protease digest. (C) Gel filtration after separation from the MBP by TEV digestion. Peaks corresponding to the MBP and E6 proteins are indicated. Note that very small amounts of monomeric E6 are recovered after gel filtration.