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. Author manuscript; available in PMC: 2016 Jan 1.
Published in final edited form as: J Biomed Mater Res A. 2014 Apr 23;103(1):409–419. doi: 10.1002/jbm.a.35188

Figure 3.

Figure 3

Heparin column purification of TAT-Gel after cleavage of thioredoxin-6×His tag from the TRX-TAT-Gel by incubation with TEV protease. (A) Chromatogram. Using a NaCl salt gradient from 0 to 1.4 M (red line), three major fractions labeled as Peak 1 – 3 eluted at 0, 0.2 and 0.7 M NaCl (with retention time of 2, 20 and 45 min, respectively). (B) SDS-PAGE results for the fractions eluted from the heparin column. Lane M: markers of the protein molecular weight standard (Mark 12™ standard, Invitrogen). Lane 1, 2, and 3 represented results from the three peak fractions (1, 2, and 3, respectively). Results showed that TAT-Gel was eluted from the 3rd peak at 0.7 M NaCl. (TRX-TAT-Gel: recombinant thioredoxin-6×His tagged-TAT-gelonin fusion protein, TAT-Gel: recombinant TAT-gelonin fusion protein)