PARTIAL PURIFICATION OF PEROXIDASE FROM IRAQI RADISH ROOTS.
- Biotechnology Research Center, Al-Nahrain University.
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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 DEAE-Cellulose 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.
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[Ayat adnan abbas and Majeed arsheed sabbah. (2017); PARTIAL PURIFICATION OF PEROXIDASE FROM IRAQI RADISH ROOTS. Int. J. of Adv. Res. 5 (Jan). 2665-2668] (ISSN 2320-5407). www.journalijar.com
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