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. 2003 Dec;185(24):7111–7119. doi: 10.1128/JB.185.24.7111-7119.2003

FIG. 1.

FIG. 1.

Purification of HupUV protein on HiTrap chelating column. Twenty microliters of each fraction (except for fraction 6, which was 10 μl) was loaded onto a 12% SDS-acrylamide gel. Lanes 1, soluble fraction; 2, nonretained fraction; 3, wash with 50 mM imidazole buffer; 4, pool of the fractions eluted at 100 mM imidazole; 5, pool of the fractions eluted at 200 mM imidazole; 6, pool of fraction 4 purified on a second HiTrap column and elution with 250 mM imidazole. Molecular masses of protein markers are indicated on the left.