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. Author manuscript; available in PMC: 2015 Oct 1.
Published in final edited form as: Protein Expr Purif. 2014 Aug 12;102:69–75. doi: 10.1016/j.pep.2014.08.005

Table 1.

Purification of (Man)5-rhChymase.

Step Total Protein
(A280)		 Total Activity
(units)		 Specific Activity
(units/A280)		 Fold-
Purification		 %
Yield
Diluted Medium 7.25 1.26×106 1.74×105 1 -
Cation Exchange 0.243 1.49×106 6.13×106 35.2 100
Heparin Affinity 0.083 1.16×106 1.40×107 80.5 78

Clarified fermentation medium (500 mL) was diluted 1:1 with dH2O prior to cation exchange chromatography. Total activity (1 unit = 1 mA410/min) reports activity for the total sample volume at each step, measured using the chymase substrate suc-AAPF-SBzl. Fold-purification demonstrates increases in specific activity relative to the diluted medium. The % yield is reported as a percentage of the total activity recovered from cation exchange. Accurate quantification of yield based on fermentation medium could not be achieved due to differences in buffer conditions and potential endogenous yeast enzymes and inhibitors.