SEARCH · PubMed Health

Results for “Benzphetamine”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources

PubMed1995

Hair analysis for drugs of abuse. XI. Disposition of benzphetamine and its metabolites into hair and comparison of benzphetamine use and methamphetamine use by hair analysis.

In order to study the disposition of benzphetamine (BZP) and its metabolites, desmethyl benzphetamine (norBZP), p-hydroxy desmethyl benzphetamine (OHnorBZP), methamphetamine (MA) and amphetamine (AP), from plasma to hair in rats, an analytical method for identifying these drugs in plasma, urine and hair was developed with selected ion monitoring of gas chromatograph/mass spectrometry (GC/MS-SIM) results. After the intraperitoneal administration of BZP to rats (10 mg/kg/d, 10d, n = 3), concentrations of BZP and its metabolites in rat hair newly grown for 4 weeks were compared to the areas under the concentration versus time curve (AUCs) of these drugs in the rat plasma. The concentrations of BZP, norBZP, OHnorBZP, MA and AP in the rat hair were 14.8 +/- 1.4, 6.1 +/- 0.3, 2.6 +/- 0.5, 2.3 +/- 0.1 and 9.2 +/- 0.3 ng/mg, and the ratio of the concentrations in the hair to AUCs in the rat plasma was 3.0:0.1:0.1:0.6:0.2, respectively. This fact suggested that BZP tends to be readily incorporated into hair from blood. The method was applied to the determination of the metabolites in scalp hair and pubic hair of humans who orally ingested BZP (30 mg/d, 5d, n = 2). BZP, norBZP, MA and AP were detected at 0.14-0.56, 0.29-0.63, 0.10 and 1.06-1.66 ng/mg in the scalp hair and at 0.10-0.20, 0.13-0.18, trace-0.15 and 0.23 ng/mg in the pubic hair, respectively. It was shown that BZP use could be retrospectively distinguished from MA use by the detection of BZP and/or norBZP in hair.

Adult↗

PubMed1983

Interaction of constitutive and phenobarbital-induced cytochrome P-450 isozymes during the sequential oxidation of benzphetamine. Explanation for the difference in benzphetamine-induced hydrogen peroxide production and 455-nm complex formation in microsomes from untreated and phenobarbital-treated rats.

The following pathway for benzphetamine (Bz) metabolism in rat hepatic microsomes was established: Bz leads to norbenzphetamine (NorBz) leads to N-hydroxynorbenzphetamine leads to N-benzylethyl-alpha-phenylnitrone leads to 2-nitroso-1-phenylpropane. The last product forms a complex with cytochrome P-450 with an absorbance maximum at 455 nm. Steps 1, 2, and 4 are cytochrome P-450-dependent; Step 3 appears to involve the flavoprotein, mixed-function amine oxidase. Step 2 is partially uncoupled, producing H2O2 at approximately 3 times the rate of N-hydroxylation. Bz is oxidized to NorBz in microsomes from both untreated rats (U-microsomes) and phenobarbital (PB)-treated rats (PB-microsomes), but the 455-nm peak does not appear in U-microsomes until almost all of the Bz has been converted to NorBz; i.e., Bz inhibits the oxidation of NorBz in U- but not in PB-microsomes. The inhibition is competitive. Bz inhibits the oxidation of the nitrone to 2-nitroso-1-phenylpropane in both U- and PB-microsomes; NorBz inhibits this reaction in U-microsomes only. These results can be explained as follows. The substrate affinities of the cytochrome P-450 primarily responsible for the N-demethylation of Bz in U- and PB-microsomes differ markedly. The constitutive cytochrome(s) in U-microsomes has a high affinity for Bz; PB induces both this form and a cytochrome(s) with a lower affinity for Bz. The substrate affinities of these two cytochromes P-450 for NorBz do not differ appreciably. Thus, although both forms of cytochrome P-450 can oxidize Bz and NorBz in PB-microsomes, Bz is primarily oxidized by the constitutive form, whereas NorBz is oxidized primarily by the induced form, thereby relieving competition and increasing the over-all sequential oxidation of Bz. The nitrone appears to be oxidized exclusively by the constitutive form in both U- and PB-microsomes. The current study shows that PB induction of monooxygenase activity need not be due entirely to an increase in the amount of cytochrome P-450 or the substrate selectivity of cytochrome P-450 isozyme(s) responsible for that activity, but that, in at least one case, the metabolism of Bz, PB-induced activity can be due, at least in part, to the induction of a cytochrome P-450 isozyme that relieves substrate inhibition.

Animals↗

PubMed1978

Enhancement in vivo of drug oxidations following administration of benzphetamine, acetone, metyrapone and dimethylsulfoxide.

Effects of benzphetamine, acetone, metyrapone and dimethylsulfoxide administration to rats on the metabolism of drugs by liver 9,000 x g supernatant fraction were studied herein. Activities for aniline hydroxylation and phenacetin O-deethylation were increased while ethylmorphine and benzphetamine N-demethylations were unchanged by the single administration of acetone, metyrapone or dimethylsulfoxide. Increase in aniline hydroxylase activity by about 53.4% and in phenacetin O-deethylase activity by about 44.4% were observed at 30 min after the single administration of benzphetamine whereas ethylmorphine N-demethylase activity was slightly decreased. NADPH-cytochrome P-450 reductase activity and cytochrome P-450 content were unaltered until 12 hr after the single administration of benzphetamine. Aniline hydroxylation was increased by the addition of benzphetamine to the incubation mixture and the increase in aniline hydroxylation caused by benzphetamine could be reversed by washing the microsomes.

Acetone↗

PubMed1988

Discriminative stimulus effects of caffeine and benzphetamine in amphetamine-trained volunteers.

The discriminative stimulus (DS) and subjective effects of caffeine (100 and 300 mg, PO) and benzphetamine (12.5 and 50 mg, PO) were studied in 18 normal human volunteers trained to discriminate between d-amphetamine (10 mg) and placebo. d-Amphetamine increased ratings of drug liking and activity level and produced a profile of subjective effects characteristic of amphetamine and related psychomotor stimulants. The DS effects of d-amphetamine generalized only partially to caffeine and benzphetamine; mean percent d-amphetamine-appropriate responding was 42 and 58 after 100 and 300 mg caffeine, respectively, and 17 and 56 after 12.5 and 50 mg benzphetamine, respectively. Neither dose of caffeine affected ratings of drug liking or activity level, but 300 mg caffeine did produce a profile of subjective effects that partially overlapped with that produced by d-amphetamine. Benzphetamine 50 mg, but not 12.5 mg, increased ratings of drug liking and activity level and produced a profile of subjective effects qualitatively similar to, but weaker than, that produced by d-amphetamine. For both caffeine and benzphetamine, a close relationship was observed between their subjective effects and their ability to substitute for the DS effects of d-amphetamine. These results correspond well with findings obtained from similar studies conducted with laboratory animals, providing further support for the reliability and validity of human drug discrimination paradigms.

Adult↗

PubMed1998

Development of a method for the quantitation of benzphetamine metabolites in human urine by high-performance liquid chromatography.

We developed a high-performance liquid chromatography (HPLC) method for quantitating p-hydroxy-N-benzylamphetamine glucuronide (pHBAG) and p-hydroxy-benzphetamine glucuronide (pHBZG), which are urinary metabolites of benzphetamine, in humans. Urine samples were hydrolysed with beta-glucuronidase (EC 3.2.1.31) at 37 degrees C overnight and the treated urine was applied to a solid phase extraction column. After washing the column with water, 0.01 mol/L acetic acid and methanol, pHBA and pHBZ were eluted with dichloromethane:isopropanol:28% ammonium hydroxide (78.4:19.6:2.0 v/v). The eluate was evaporated and the residue was dissolved in acetonitrile: 5 mmol/L 1-pentane sulphonic acid (5:95 v/v) and analysed by HPLC with gradient elution. The amounts of urinary pHBAG and pHBZG excreted by two human subjects after oral administration of 10 mg benzphetamine hydrochloride were determined. About 10-15% of benzphetamine was found to be excreted as pHBAG and pHBZG, and almost all of these metabolites were excreted within 24 h. Urine samples should be collected as early as possible after ingestion of benzphetamine to detect pHBAG and pHBZG.

Administration, Oral↗

PubMed2004

Mechanistic studies with N-benzyl-1-aminobenzotriazole-inactivated CYP2B1: differential effects on the metabolism of 7-ethoxy-4-(trifluoromethyl)coumarin, testosterone, and benzphetamine.

Mechanistic studies with N-benzyl-1-aminobenzotriazole (BBT)-inactivated cytochrome P450 2B1 were conducted to determine which step(s) in the reaction cycle had been compromised. Stopped-flow studies, formation of the oxy-ferro intermediate, and analysis of products suggested that the reductive process was slower with the BBT-modified enzyme. The reduced rate of reduction alone could not account for the loss in 7-ethoxy-4-(trifluoromethyl)coumarin (EFC) O-deethylation or testosterone hydroxylation activity. Surprisingly, the ability of the BBT-modified enzyme to generate formaldehyde from benzphetamine was much less affected. Benzphetamine metabolite analysis by electrospray ionization-mass spectrometry showed that the BBT-modified enzyme had a slightly greater propensity towards aromatic hydroxylation together with reduced levels of N-demethylation and little change in the N-debenzylation of benzphetamine. Orientation of substrates within the active site of the BBT-inactivated enzyme may be affected such that the more flexible benzphetamine can be metabolized, whereas metabolism of rigid, planar molecules such as EFC and testosterone is hindered.

Anaerobiosis↗

PubMed1989

Site-directed mutageneses of rat liver cytochrome P-450d: catalytic activities toward benzphetamine and 7-ethoxycoumarin.

Catalytic activities toward benzphetamine and 7-ethoxycoumarin of 11 distal mutants, 9 proximal mutants, and 3 aromatic mutants of rat liver cytochrome P-450d were studied. A distal mutant Thr319Ala was not catalytically active toward benzphetamine, while this mutant retained activity toward 7-ethoxycoumarin. Distal mutants Gly316Glu, Thr319Ala, and Thr322Ala displayed higher activities (kcat/Km) toward 7-ethoxycoumarin that were 2.4-4.7-fold higher than that of the wild-type enzyme. Although kcat/Km values of four multiple distal mutants toward benzphetamine were less than half that of the wild type, activities of these mutants toward 7-ethoxycoumarin were almost the same as or higher than the wild-type activity toward this substrate. The distal double mutant Glu318Asp, Phe325Tyr showed 6-fold higher activity than the wild-type P-450d toward 7-ethoxycoumarin. Activities of the proximal mutants Lys453Glu and Arg455Gly toward both substrates were much lower (less than one-seventh) than the corresponding wild-type activities. Catalytic activities of three aromatic mutants, Phe425Leu, Pro427Leu, and Phe430Leu, toward benzphetamine were less than 7% of that of the wild type, while the activities of these aromatic mutants toward 7-ethoxycoumarin were more than 2.5 times higher than the wild-type activity toward this substrate. From these findings, in conjunction with a molecular model for P-450d, we suggest that (1) the relative importance to catalysis of various distal helix amino acids differs depending on the substrate and that these differences are associated with the size, shape, and flexibility of the substrate and (2) the proximal residue Lys453 appears to play a critical role in the catalytic activity of P-450d, perhaps by participating in forming an intermolecular electron-transfer complex.

Amino Acid Sequence↗

PubMed1995

The stoichiometry of the cytochrome P-450-catalyzed metabolism of methoxyflurane and benzphetamine in the presence and absence of cytochrome b5.

The complete stoichiometry of the metabolism of the cytochrome b5 (cyt b5)-requiring substrate, methoxyflurane, by purified cytochrome P-450 2B4 was compared to that of another substrate, benzphetamine, which does not require cyt b5 for its metabolism. Cyt b5 invariably improved the efficiency of product formation. That is, in the presence of cyt b5 a greater percentage of the reducing equivalents from NADPH were utilized to generate substrate metabolites, primarily at the expense of the side product, superoxide. With methoxyflurane, cyt b5 addition always resulted in an increased rate of product formation, while with benzphetamine the rate of product formation remained unchanged, increased or decreased. The apparently contradictory observations of increased reaction efficiency but decrease in total product formation for benzphetamine can be explained by a second effect of cyt b5. Under some experimental conditions cyt b5 inhibits total NADPH consumption. Whether stimulation, inhibition, or no change in product formation is observed in the presence of cyt b5 depends on the net effect of the stimulatory and inhibitory effects of cyt b5. When total NADPH consumption is inhibited by cyt b5, the rapidly metabolized, highly coupled (approximately equal to 50%) substrate, benzphetamine, undergoes a net decrease in metabolism not counterbalanced by the increase in the efficiency (2-20%) of the reaction. In contrast, in the presence of the slowly metabolized, poorly coupled (approximately equal to 0.5-3%) substrate, methoxyflurane, inhibition of total NADPH consumption by cyt b5 was never sufficient to overcome the stimulation of product formation due to an increase in efficiency of the reaction.

Animals↗

PubMed1995

Localization of the epitope in methamphetamine and its antibody use for the detection of methamphetamine and benzphetamine by polarization fluoroimmunoassay.

An antibody was prepared, using a four carbon-bridged methamphetamine molecule as an immunogen in order to develop a polarization fluoroimmunoassay for urine screening of methamphetamine and benzphetamine. Also, its binding characteristics were investigated to locate epitope sites of methamphetamine. The study showed that the antibody was highly capable of eliciting a polarization fluoroimmunoassay response. However, the detection limit was much greater for benzphetamine (0.05 ppm) than for methamphetamine (0.2 ppm) and weakly antibody binding was found with methamphetamine. This difference in sensitivity may reflect the similarity of benzphetamine to the immunogen used to produce the antibody. Both benzphetamine and the immunogen have a tertiary amine attached to a carbon bridges whereas methamphetamine has only a secondary amine and amphetamine has a primary amine group. The difference of cross-reactivity data between phenylethylamine drugs and beta-hydroxyl phenylethylamine drugs indicates that the beta-carbon position have a major influence on the antibody interaction. Thus, the substitution of hydroxyl group on beta-carbon resulted in virtually no antibody affinity, even if a tertiary amine or secondary amine group was present in the molecule. This suggests that the beta-carbon chain plays a primary role as the epitope site with cooperative binding site of tertiary amine or secondary amine in alpha-carbon position. A hydroxyl group at the beta-carbon position plays an important inhibitory role to the antibody binding.

Antibody Affinity↗

PubMed1986

The metabolism of 1-phenyl-2-(N-methyl-N-benzylamino)propane (benzphetamine) and 1-phenyl-2-(N-methyl-N-furfurylamino)propane (furfenorex) in man.

The metabolic fate of 1-phenyl-2-(N-methyl-N-benzylamino)propane (benzphetamine) and 1-phenyl-2-(N-methyl-N-furfurylamino)propane (furfenorex) in healthy volunteers has been investigated. Nine metabolites with traces of the unchanged drug were detected in human urine after oral administration of benzphetamine, and five metabolites were found following administration of furfenorex. The major metabolites were 1-(p-hydroxyphenyl)-2-(N-benzylamino)propane for benzphetamine and 1-phenyl-2-(N-methyl-N-gamma-valerolactonylamino)propane for furfenorex. In both cases, methamphetamine, amphetamine and their hydroxylated metabolites were also excreted as minor metabolites. Identified metabolites excreted in three days after administration of benzphetamine accounted for 30-44% of the dose and those excreted after administration of furfenorex, 31-46%.

Administration, Oral↗

PubMed1994

Stimulatory effects of lung cytochrome b5 on benzphetamine N-demethylation in a reconstituted system containing lung cytochrome P450LgM2.

Cytochrome b5 was partially purified from sheep lung microsomes in the presence of detergents Emulgen 913 and cholate by three consecutive DEAE-cellulose and Sephadex G-100 gel filtration chromatographies. The specific content of cytochrome b5 was 16.5 nmol/mg protein and purified cytochrome b5 fractions were free of cytochrome P450, NADPH-cytochrome P450 reductase and NADH-cytochrome b5 reductase activities. The influences of increasing concentrations of lung cytochrome b5 on benzphetamine N-demethylation reactions were examined in four different reconstitution systems containing lung cytochrome P450LgM2, lung cytochrome P450 reductase and lipid. In each system concentration of reductase was doubled with respect to former system. In all systems cytochrome b5 stimulated benzphetamine N-demethylase activity especially when cytochrome b5 was present at 0.5:1 molar ratio with respect to cytochrome P450LgM2. Besides, the greatest fold of increase in benzphetamine N-demethylation activity due to addition of cytochrome b5 was observed in System 1 with the lowest concentration of reductase.

Animals↗

PubMedDate not supplied

Detection of amphetamine and methamphetamine following administration of benzphetamine.

Interpretation of urine drug-testing results is a challenging endeavor for several reasons. Effects of pH, dilution, legitimate and illicit sources of the drugs, and, perhaps the most challenging, the possibility of the methamphetamine and/or amphetamine being the result of the use of some other drug. Although it is known that 14 different compounds are metabolized to methamphetamine or amphetamine or both, there is little information on the metabolic profile of many of these compounds, making interpretation of results difficult. Benzphetamine, administered as a single Didrex tablet, was given to 10 subjects (7 male and 3 female) and urine samples collected for the next 7 days. Gas chromatography-mass spectrometry results showed 3 of the 10 subjects did not have a single urine sample that exceeded a 500-ng/mL cutoff for amphetamine or methamphetamine. The other subjects had between one and six samples that tested positive at or above that level. Two subjects excreted more methamphetamine than amphetamine, whereas the other eight excreted greater amounts of amphetamine than methamphetamine. The observed ratio between amphetamine and methamphetamine was significantly different than what would be expected from the use of methamphetamine. Results of this study indicate the metabolism of benzphetamine to desmethylbenzphetamine is a major pathway in the metabolism of the drug. Enantiomer analysis of the methamphetamine and amphetamine revealed only the d-enantiomer. Results of this study add significant information useful to interpret the possibility of benzphetamine as the origin of methamphetamine and amphetamine in urine samples.

Adult↗

PubMed1993

The role of cytochrome P450 3A (CYP3A) isoform(s) in oxidative metabolism of testosterone and benzphetamine in human adult and fetal liver.

Testosterone metabolism was studied in human adult and fetal liver microsomes. In fetal livers 6 beta-hydroxylase (6 beta OH) activity (1-2% of adult activity) and 2 alpha-hydroxylase (2 alpha OH) activity (about 40% of adult activity) were present. Also some fetal livers produced two unknown metabolites. Androstenedione was formed in all fetal livers studied (10-20% of adult activity). Testosterone hydroxylations at 6 beta-, 2 beta-, 15 alpha- and 15 beta-positions were associated with CYP3A isoform(s) in adult liver, because they were strongly inhibited by midazolam, a known substrate for CYP3A4 and by anti-CYP3A4 antibody. Fetal liver activities were consistently inhibited less than the activities in adult livers. The formation of androstenedione was not affected by these inhibitors in fetal or adult liver microsomes. Benzphetamine N-demethylase activity in the fetal livers was about 40% of adult activity. Anti-CYP3A4 antibody had no effect on that activity in fetal or in adult liver microsomes, whereas a monoclonal antibody 1-68-11 (generated against rat CYP2C11) slightly inhibited benzphetamine N-demethylase activity in adult liver. This study indicates that human fetal and adult liver are dissimilar in their testosterone metabolism pattern. The formation of androstenedione from testosterone in fetal liver may have a physiological role. Testosterone hydroxylases are less inhibited by anti-CYP3A4 antibody, midazolam and progesterone in fetal than in adult liver.

Adult↗

PubMed1982

The metabolism of 1-phenyl-2-(N-methyl-N-benzylamino)propane (benzphetamine) in vivo in the rat.

1. The metabolism of 1-phenyl-2-(N-methyl-N-benzylamino)propane (benzphetamine) was studied in vivo in the rat. 2. Nine metabolites were obtained from urine after oral administration of benzphetamine to rats. The major metabolite, identified as 1-(p-hydroxyphenyl)-2-(N-benzylamino)propane, was formed by aromatic hydroxylation and N-demethylation. One of the minor metabolites was methamphetamine, formed by N-debenzylation. 3. Metabolites excreted in three days after administration of the drug amounted to about 40% of the dose.

Administration, Oral↗

PubMed1983

The metabolism of 1-phenyl-2-(N-methyl-N-benzylamino)propane (benzphetamine) in vitro in rat.

The metabolism of 1-phenyl-2-(N-benzylamino)propane (benzphetamine) in vitro was studied using rat-liver microsomes. Five metabolites were isolated from the incubation mixture and identified as 1-phenyl-2-(N-benzylamino)propane (benzylamphetamine), (1-(p-hydroxyphenyl)-2-(N-methyl-N-benzylamino)propane, 1-(p-hydroxyphenyl)-2-(N-benzylamino)propane, methamphetamine and amphetamine. This metabolism in vitro was compared with that in vivo which was reported previously. The formation of all five metabolites were catalysed by liver microsomes supplemented with NADPH and O2, and inhibited by either SKF 525-A or CO. N-Demethylation was inhibited by either 2-methyl-1,2-bis-(3-pyridyl)-1-propanone (metyrapone) or n-octylamine, while aromatic hydroxylation was inhibited by 7,8-benzoflavone and N-debenzylation was depressed by all these inhibitors. N-Demethylation was enhanced by pretreatment of rats with phenobarbitone, while aromatic hydroxylation was induced by pretreatment with 3-methylcholanthrene, and N-debenzylation was Induced by pretreatment with either phenobarbitone or 3-methylcholanthrene. These data suggested that the metabolism of benzphetamine was mediated by three slightly different enzyme systems.

Amphetamines↗

PubMed1983

Monooxygenase activities of dioxygenases. Benzphetamine demethylation and aniline hydroxylation reactions catalyzed by indoleamine 2,3-dioxygenase.

Benzphetamine demethylase and aniline hydroxylase activities were determined with various hemoproteins including indoleamine 2,3-dioxygenase in a cytochrome P-450-like reconstituted system containing NADPH, NADPH-cytochrome P-450 reductase, and O2. The highest specific activities, almost comparable to those of liver microsomal cytochrome P-450, were detected with indoleamine 2,3-dioxygenase from the rabbit intestine. The indoleamine 2,3-dioxygenase-catalyzed benzphetamine demethylation reaction was inhibited by catalase but not by superoxide dismutase. Exogenous H2O2 or organic hydroperoxides was able to replace the reducing system and O2. The stoichiometry of H2O2 added to the product formed was essentially unity. These results indicate that the dioxygenase catalyzes the demethylation reaction by the so-called "peroxygenation" mechanism using H2O2 generated in the reconstituted system. On the other hand, the dioxygenase-catalyzed aniline hydroxylation reaction was not only completely inhibited by catalase but also suppressed by superoxide dismutase by about 60%. Although the O2- and H2O2-generating system (e.g. hypoxanthine-xanthine oxidase) was also active as the reducing system, neither exogenous H2O2 nor the generation of O2- in the presence of catalase supported the hydroxylation reaction, indicating that both H2O2 and O2- were essential for the hydroxylation reaction. However, typical scavengers for hydroxyl radical and singlet oxygen were not inhibitory. These results suggest that a unique, as yet unidentified active oxygen species generated by H2O2 and O2- participates in the dioxygenase-mediated aniline hydroxylation reaction.

Aniline Compounds↗

PubMed1983

Correlations between spin equilibrium shift, reduction rate, and N-demethylation activity in liver microsomal cytochrome P-450 and a series of benzphetamine analogues as substrates.

Cytochrome P-450 forms a thermal ferric spin equilibrium which is significantly shifted by substrate binding. Within a series of benzphetamine analogues the liver microsomal enzyme system exhibits a close correlation of the substrate induced spin equilibrium shift towards the high spin state and both the rate of P-450 reduction, and of substrate turnover, as well. The spin equilibrium regulates the first electron transfer by favoured high spin state reduction and rapid pre-equilibration with respect to the low spin fraction.

Animals↗

PubMed1985

Spin state control of cytochrome P-450 reduction and catalytic activity in a reconstituted P-450 LM2 system as induced by a series of benzphetamine analogues.

Reconstituted liposomal cytochrome P-450 LM2 was reacted with a series of benzphetamine analogues as substrates. Based on the thermodynamical model of Ristau et al. (Biochim. Biophys. Acta, 536 (1978) 226-234) the free enthalpy of substrate binding to the high spin form of the enzyme was shown to correlate with the total high spin content of the respective enzyme substrate complex. Reduction and substrate N-demethylation rates as well have been evidenced to linearly correlate with the substrate-induced spin shift delta alpha and moreover with the spin content alpha. The data obtained provide further experimental support for the spin state regulation of the reduction and conversion rate of cytochrome P-450 LM2.

Animals↗