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. Author manuscript; available in PMC: 2011 Nov 1.
Published in final edited form as: Peptides. 2010 Aug 14;31(11):1957–1965. doi: 10.1016/j.peptides.2010.08.008

Figure 2.

Figure 2

A. Fermentation profile of a 10 L high-density fermentation of SUMO-IDR-1 using glucose-feed and IPTG induction for 14h. The fermentation yielded 1.5 kg biomass.

B. Comparison of the RP-chromatography profile for both the synthetic (upper panel) and recombinant IDR-1 peptide (lower panel). Both peptides eluted at the same percent of acetonitrile.

C. MALDI analysis of the purified IDR-1 peptide as well as the remaining his-SUMO protein after cleavage. The determined mass for IDR- 1 was identical to the synthetic peptide and the correct mass for his-sumo revealed 100 % cleavage using its protease sumoase. The MS profile for IDR-1 was magnified for better visualization.

D. Tricine-SDS-PAGE separation of the proteins from the recovered fractions from RP-chromatography shown in figure 2B. As can be seen in lanes 1 and 2, pure IDR-1 was recovered from fractions 11 and 12 followed by elution of SUMO in lanes 3–10). Lane 5 shows the Kaleidoscope Marker Plus (BioRAD).