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. 2014 Feb 21;15(2):3204–3219. doi: 10.3390/ijms15023204

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© 2014 by the authors; licensee MDPI, Basel, Switzerland

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 2. — Purification of 75 kDa gelatinase from TYS culture. (A) Diethylaminoethyl (DEAE)-anion-exchange chromatography of extracellular protein from TYS (solid line) and YS (dot line) cultures. The bar indicates the protease activity using hemoglobin as the substrate; and (B) Hydrophobic affinity chromatography of the protease activity fractions eluted from DEAE chromatography. Fr1 and Fr2 protease activity fractions (dashed bars) were analyzed by SDS-PAGE (b1 insert) and gelatin-SDS zymogram (b2 insert).

Figure 2. — Purification of 75 kDa gelatinase from TYS culture. (A) Diethylaminoethyl (DEAE)-anion-exchange chromatography of extracellular protein from TYS (solid line) and YS (dot line) cultures. The bar indicates the protease activity using hemoglobin as the substrate; and (B) Hydrophobic affinity chromatography of the protease activity fractions eluted from DEAE chromatography. Fr1 and Fr2 protease activity fractions (dashed bars) were analyzed by SDS-PAGE (b1 insert) and gelatin-SDS zymogram (b2 insert).