منابع مشابه
The effect of NADPH concentration on the reduction of cytochrome P-450 LM2.
Cytochrome P-450 LM2 reduction was measured at a series of NADPH concentrations in the absence of substrate and in the presence of 1 mM benzphetamine. In the absence of substrate reduction could be described as a biphasic process with 55% of the reaction occurring in the first phase (at 20 microM NADPH). When benzphetamine was present, the fraction of the reaction occurring in the first phase w...
متن کاملTemperature Dependence of Cytochrome P-450 Reduction
The NADPH-dependent reduction of rat hepatic microsomal cytochrome P-450 has been studied as a function of temperature. In the temperature range 4-37’ the reduction reaction was found to be biphasic and composed of two concurrent first order processes. This phenomenon was observed with microsornes from untreated and phenobarbital-induced animals in the presence or absence of exogenous Type I su...
متن کاملNADPH: cytochrome P-450 reductase in olfactory epithelium. Relevance to cytochrome P-450-dependent reactions.
The presence of a very active cytochrome P-450-dependent drug-metabolizing system in the olfactory epithelium has been confirmed by using 7-ethoxycoumarin, 7-ethoxyresorufin, hexobarbitone and aniline as substrates, and the reasons for the marked activity of the cytochrome P-450 in this tissue have been investigated. The spectral interaction of hexobarbitone and aniline with hepatic and olfacto...
متن کاملCompetition between cytochrome P-450 isozymes for NADPH-cytochrome P-450 oxidoreductase affects drug metabolism.
NADPH-cytochrome P-450 oxidoreductase (CPR) is essential for the catalytic activity of cytochrome P-450 (P-450). On a molar basis, the amount of P-450 exceeds that of CPR in human liver. In this study, we investigated whether drug-drug interactions can occur as a result of competition between P-450 isozymes for this ancillary protein. For this purpose, combinations of P-450 isozymes were coexpr...
متن کاملCharacterization of a phenobarbital - inducible cytochrome P - 450 , NADPH - cytochrome P - 450 reductase and reconstituted cytochrome P - 450 mono - oxygenase system from rat brain
Cytochrome P-450 was purified to apparent homogeneity from the brain microsomes of phenobarbital-treated rats. The specific content of the purified P-450 was 12.7 nmol/mg of protein. NADPH-cytochrome P-450 reductase (reductase) was also purified to apparent homogeneity from brain microsomes. The specific content was 34.7,mol of cytochrome c reduced/min per mg of protein. The reduced carbon mono...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)83341-5