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- W2187837503 abstract "Cytochrome P-450 waspurified toapparent homogeneity fromthebrain microsomes ofphenobarbital-treated rats. The specific content ofthepurified P-450 was12.7 nmol/mg ofprotein. NADPH-cytochrome P-450 reductase (reductase) was alsopurified toapparent homogeneity frombrain microsomes. Thespecific content was34.7 ,molofcytochrome c reduced/min permgofprotein. Thereduced carbon monoxide spectrum ofpurified P-450exhibited apeakat450nm. BoththeP-450 andthereductase movedassingle bands onSDS/PAGE. Themolecular masses ofthepurified P-450 and thereductase weredetermined tobe53.3and72.0 kDarespectively. Thepurified brain P-450cross-reacted with antibodies toratliver P-4501IB1/11B2 whenexamined byWestern immunoblotting, butnoimmunological similarity was observed with ratliver P-450IA1/A2 orP-45011E1. Purified ratbrain reductase cross-reacted withantibodies toratliver reductase. Further, immunoblot experiments withuntreated ratandhumanbrain microsomes using antisera tothe purified ratbrain P-450 andreductase indicated that these forms ofP-450 andNADPH-cytochrome P-450 reductase exist constitutively inratandhumanbrain. Purified ratbrain P-450wasreconstituted withpurified NADPH-cytochrome P-450reductase, deoxycholate anddilauroyl glyceryl 3-phosphocholine. NADPH-dependent N-demethylation of aminopyrine andmorphine wasobserved inthereconstituted system. Thecatalytic-centre activities were80.25 and 38.2 nmolofformaldehyde formed/min pernmolofP-450respectively. Thereconstituted system hadacomparatively lower catalytic-centre activity for7-ethoxycoumarin O-de-ethylase (10.5 nmolofproduct formed/min pernmolofP-450)." @default.
- W2187837503 created "2016-06-24" @default.
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- W2187837503 date "1992-01-01" @default.
- W2187837503 modified "2023-09-26" @default.
- W2187837503 title "Evidence forconstitutive presenceinratandhumanbrain" @default.
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