Immunochemical Evidence for an Association of Heme Oxygenase with the Microsomal Electron Transport System

摘要: Abstract The relationship between spleen and liver microsomal heme oxygenase activities the electron transport system requiring NADPH cytochrome P-450 has been demonstrated by immunochemical techniques. An antibody preparation to purified, homogeneous NADPH-cytochrome c reductase (NADPH-cytochrome oxidoreductase, EC 1.6.2.3) was shown inhibit concomitantly in rat pig preparations. Previous work requirement for this enzymic activity reduction of associated with drug hydroxylation reactions steroid metabolism concomitant inhibition these various anti-NADPH-cytochrome γ-globulin. levels both reported present study are less than 10% those found liver. Even at levels, however, is sufficient maintain flux required under conditions which catabolism maximal. Methemalbumin treatment rats resulted a 3.7-fold increase hepatic inhibited anti-reductase γ-globulin, indicating that induced enzyme maintained its system. Comparison paramagnetic resonance spectra ethyl isocyanide difference microsomes from untreated methemalbumin-treated failed demonstrate induction new moiety as result vivo administration methemalbumin, substrate methemalbumin did not an components system, i.e. or content, modulation control mechanisms differ governing noncompetitive binding Type I II drugs In addition studies, temporal among decrease magnitude hexobarbital, activity, measurable reversal parameters during recovery phase following single injection strongly indicates involvement same systems