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NADPH-Cytochrome P450 reductase (CPR) is a key enzyme catalyzing electron transfer in detoxification metabolism. In this study, two methods were employed to purify CPR enzyme from turkey liver microsomes. In the first method, NADPH-Cytochrome P450 reductase was purified using 2ʹ, 5ʹ-ADP Sepharose 4B affinity column with ~114 purification fold and ~23% yield. In the second method, CPR was purified using DE-52 Cellulose anion exchange column and 2ʹ, 5ʹ-ADP Sepharose 4B affinity column with 124 purification fold and 8% yield. Enzyme purity was checked in both methods with SDS-PAGE. Characteristics kinetic features of the purified enzyme were identified. The effects of some metal ions on purified PCR enzyme activity have been investigated in vitro conditions. It has been found that Ag+, Hg2+ and Cu2+ metal ions have an inhibitory effect on CPR enzyme activity.

Hindi Karaciğerinden NADPH-Sitokrom P450 Redüktaz’ın Saflaştırılması, Karakterizasyonu ve Bazı Metal İyonlarının Enzim Aktivitesi Üzerindeki Etkileri