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. 2016 Aug 23;11(8):e0161697. doi: 10.1371/journal.pone.0161697

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© 2016 Lai et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 2 — A. SDS-PAGE of Ni-NTA affinity purification of recombinant TYR456 and 6xHis-tag cleavage. M, molecular weight marker; MD, concentrated medium; FT, flow-through fraction; W, wash fraction; E, elution fraction; TC, TEV-protease cleaved fraction. B. Ion exchange chromatogram of TYR456, upon applying a NaCl gradient from 50 mM to 500 mM. Two elution peaks are observed (A and B), both corresponding to recombinant tyrosinase samples. Peak B eluting at ~150 mM NaCl was selected for further analysis.