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. 2018 Feb 2;293(12):4230–4243. doi: 10.1074/jbc.RA117.001238

Figure 2.

Figure 2.

Purification of recombinant HCLase Er from E. coli by Ni2+-chelation chromatography. Enzyme purity following each fractionation step was assessed by SDS-PAGE using 13.2% polyacrylamide gels followed by staining with Coomassie Brilliant Blue. Lane 1, unstained protein molecular weight marker SM 0431 (Thermo Fisher Scientific); lane 2, uninduced cell lysate; lane 3, induced cell lysate; lane 4, supernatant fluid of the induced cell lysate; lane 5, purified recombinant HCLase Er. Ten microliters of corresponding sample containing about 10 μg of protein was individually loaded on lanes 1–4, and 1 μg of purified enzyme was loaded on lane 5. Molecular mass markers and their corresponding masses are indicated.