Journals / Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi / 2018 / Cilt: 8 - Sayı: 3
Purification, Characterization of NADPH-Cytochrome P450 Reductase from Turkey Liver and Effects of Some Metal Ions on Enzyme Activity
- Pages
- 183–189
- DOI
- —
Abstract
NADPH-Cytochrome P450 reductase (CPR) is a key enzyme catalyzing electron transfer indetoxification metabolism. In this study, two methods were employed to purify CPR enzyme from turkey livermicrosomes. In the first method, NADPH-Cytochrome P450 reductase was purified using 2ʹ, 5ʹ-ADP Sepharose 4Baffinity column with ~114 purification fold and ~23% yield. In the second method, CPR was purified using DE-52Cellulose 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 purifiedenzyme were identified. The effects of some metal ions on purified PCR enzyme activity have been investigatedin vitro conditions. It has been found that Ag+, Hg2+ and Cu2+ metal ions have an inhibitory effect on CPR enzymeactivity.
Özet
NADPH-Sitokrom P450 redüktaz (CPR) enzimi, detoksifikasyon metabolizmasında elektron transferini