LAUSR

Received: 01 December 2016 Final Accepted: 29 December 2016 Published: January 2017 Peroxidases (EC 1.11.1.7) are enzymes whose primary function is to oxidize a variety of hydrogen donor at the expense of hydrogen peroxide. In the present study, peroxidase was partially purified from Iraqi radish. Crude extract was prepared by blending and centrifugation of local radish roots. The enzyme was salt precipitated using 80% ammonium sulfate, dialyzed and then partially purified using DEAECellulose ion exchange chromatography. Two fractions of peroxidase activity were eluted; the first was purified 35.62 folds and showed a final specific activity 41.85U/mg with a 51.29% yield. The second was purified 23.45 folds and showed a final specific activity 27.551U/mg with a 42.12% yield.