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. Author manuscript; available in PMC: 2014 Nov 28.
Published in final edited form as: J Control Release. 2013 Aug 23;172(1):10.1016/j.jconrel.2013.08.016. doi: 10.1016/j.jconrel.2013.08.016

Fig. 3.

Fig. 3

Expression and purification of rG-L. (A) SDS-PAGE and western blot assay results for rTRX-G-L. Lane M: markers of the protein molecular weight standard (Invitrogen). Lane 1 represents rTRX-G-L purified by Ni-NTA column. Lane W: western blot assay result for the rTRX-G-L; (B) SDS-PAGE analysis of the fractions from the heparin column. Eluent from the Ni-NTA column containing rTRX-G-L was incubated with TEV protease to cleave the thioredoxin-6×His tag and then applied to a heparin column with NaCl gradient. Lane M: markers of the protein molecular weight standard (Invitrogen). Lane 1, 2 and 3 represented results from the three peak fractions (1, 2, and 3, respectively). Chromatogram is shown in Fig. S4. Results showed that rG-L was eluted from the 3rd peak at 0.8 M NaCl. (rTRX-G-L: recombinant N-terminal 6×His tagged gelonin-LMWP chimera)