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. Author manuscript; available in PMC: 2015 Apr 1.
Published in final edited form as: Free Radic Biol Med. 2014 Jan 25;69:129–135. doi: 10.1016/j.freeradbiomed.2014.01.020

Table 1.

Purification of sulfhydryl oxidase from adult bovine serum

Steps Total protein (mg) A280/A456 Total activity (nmol H2O2/min) Yield (%) Specific activity (nmol/min·mg) Fold purification
Serum (500 mL diluted 5-fold) 31350 140 4148 100 0.132 1
Cation exchange (salt gradient) 10.3 31 1686 411 164 1240
Hydrophobic interaction 1.52 22 560 13.5 369 2793
Cation exchange (pH gradient) 0.57 12 402 10 706 5345
1

During loading the 2.5 L of diluted serum, the cation exchange column was intentionally overloaded as described in Methods. Without such overloading 82% of the sulfhydryl oxidase applied to the column could be recovered from the salt gradient in a single peak of enzyme activity.