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. Author manuscript; available in PMC: 2009 Dec 1.
Published in final edited form as: Protein Expr Purif. 2008 Aug 7;62(2):216–222. doi: 10.1016/j.pep.2008.07.014

Figure 1.

Figure 1

DEAE-Sepharose column chromatography: protein concentration and peroxidase activity profiles. KME Buffer A was pumped through the column at 1.0 mL/min, with 10-mL fractions being collected. The linear elution gradient (0-100% KME Buffer B) was started at fraction 16 and continued to fraction 32, 100% Buffer B being used thereafter. Protein level was measured by absorbance at 280 nm (solid line). Enzymatic activity was determined by coupled spectrophotometric assay, using CuOOH (○) or PCOOH (▲) as the peroxide substrate. One unit (U) of activity corresponds to 1 μmol of CuOOH or PCOOH consumed per min. Bar indicates fractions that were pooled for further purification.