Effect of modification of sheep lung cytochrome P450LgM2(2B) by ethylacetimidate in hydroxylation activity
BIOCHEMICAL ARCHIVES, cilt.14, sa.4, ss.241-246, 1998 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 14 Sayı: 4
- Basım Tarihi: 1998
- Dergi Adı: BIOCHEMICAL ARCHIVES
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.241-246
- Orta Doğu Teknik Üniversitesi Adresli: Evet
Özet
Cytochrome P450LgM2(2B) purified from sheep lung microsomes was treated chemically using ethylacetimidate at pH 8.5 for 2 hours at room temperature. Ethylacetimidate modification of essential lysine residues of lung P450LgM2 caused an inhibition of catalytic activity P450 towards substrate benzphetamine. Benzphetamine N-demethylase activity of the reconstituted system containing modified P450LgM2 and purified sheep lung NADPH-cytochrome P450 reductase was inhibited by 93%. This inhibition may be due to an impaired interaction of P450LgM2 and reductase via electrostatic farces.