Effect of modification of sheep lung cytochrome P450LgM2(2B) by ethylacetimidate in hydroxylation activity

Adali O.

BIOCHEMICAL ARCHIVES, vol.14, no.4, pp.241-246, 1998 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 14 Issue: 4
  • Publication Date: 1998
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.241-246
  • Middle East Technical University Affiliated: Yes


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.