PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7587934-1 1995 The kinetics of mechanism-based inactivation of phenobarbital-inducible rabbit hepatic cytochromes P450 2B4 and 2B5 by N-benzyl-(BBT) and N-alpha-methylbenzyl (alpha MB) 1-aminobenzotriazole were investigated using reconstituted P450 2B4, a stable heterologous expression system, and hepatic microsomes. Phenobarbital 48-61 cytochrome P450 2B4 Oryctolagus cuniculus 99-115 10936227-3 2000 The nature of CYP isoforms involved in this covalent binding was investigated by using cultured rabbit hepatocytes treated or not with various CYP inducers (CYP1A1/2 by beta-naphthoflavone, CYP2B4 by phenobarbital, CYP3A6 by rifampicine, CYP4A by clofibrate) and human liver and bronchial CYP-expressing cells. Phenobarbital 200-213 cytochrome P450 2B4 Oryctolagus cuniculus 190-196 19588850-4 2009 Addition of antiserum against CYP2B4, a constitutive and PB-inducible rabbit P450 isoform, to a microsomal incubation system resulted in almost complete inhibition of the formation of 3-OH-, 4-OH- and 3,4-diOH-metabolites. Phenobarbital 57-59 cytochrome P450 2B4 Oryctolagus cuniculus 30-36 7587934-4 1995 Preincubation of phenobarbital-induced hepatic microsomes with BBT and alpha MB resulted in concentration-dependent decreases in marker activities of P450 2B4 and 2B5, benzyloxyresorufin O-debenzylase and androstenedione 15 alpha-hydroxylase, respectively. Phenobarbital 17-30 cytochrome P450 2B4 Oryctolagus cuniculus 150-166 7840628-1 1995 At low levels of phenobarbital induction two forms of isoenzyme 2 (LM2; CYP2B4) were obtained during purification of cytochrome P450 from rabbit liver microsomes. Phenobarbital 17-30 cytochrome P450 2B4 Oryctolagus cuniculus 72-78 2828114-0 1988 Surface enhanced resonance Raman study of phenobarbital-induced rabbit liver cytochrome P-450 LM2. Phenobarbital 42-55 cytochrome P450 2B4 Oryctolagus cuniculus 77-97 7808429-2 1994 In this investigation, we examined the frequency of the P450 2B5-null phenotype and the functional consequences of polymorphic P450 2B5 expression in hepatic microsomes from phenobarbital-treated rabbits. Phenobarbital 174-187 cytochrome P450 2B4 Oryctolagus cuniculus 127-135 1435745-3 1992 Formation of catechol and sesamol from MDB in microsomal incubation mixtures was enhanced about 5- and 3-fold, respectively, by pretreatment of the rabbits with phenobarbital, which induced CYP2B4 and CYP4B1. Phenobarbital 161-174 cytochrome P450 2B4 Oryctolagus cuniculus 190-196 1435745-10 1992 Reconstitution experiments with CYP2B4 suggested that phenobarbital-inducible complex formation from MDA was not due to the carbene pathway involving the methylenedioxy group but was due to oxidation of the amino group. Phenobarbital 54-67 cytochrome P450 2B4 Oryctolagus cuniculus 32-38 1678603-9 1991 These results indicate that the PB-inducible isozymes such as CYP2B4 appear to play an important role in MDB demethylenation, whereas MDA and MDMA oxidation is mediated mainly by constitutive isozymes. Phenobarbital 32-34 cytochrome P450 2B4 Oryctolagus cuniculus 62-68 2125940-16 1990 When sheep lung cytochrome P-450LgM2 and P-450LM2 purified from liver of phenobarbital (PB)-induced rabbit were subjected to Western Blotting and visualized immunochemically with anti-P-450LM2, they showed identical mobilities. Phenobarbital 73-86 cytochrome P450 2B4 Oryctolagus cuniculus 41-49 2125940-16 1990 When sheep lung cytochrome P-450LgM2 and P-450LM2 purified from liver of phenobarbital (PB)-induced rabbit were subjected to Western Blotting and visualized immunochemically with anti-P-450LM2, they showed identical mobilities. Phenobarbital 73-86 cytochrome P450 2B4 Oryctolagus cuniculus 184-192 2125940-16 1990 When sheep lung cytochrome P-450LgM2 and P-450LM2 purified from liver of phenobarbital (PB)-induced rabbit were subjected to Western Blotting and visualized immunochemically with anti-P-450LM2, they showed identical mobilities. Phenobarbital 88-90 cytochrome P450 2B4 Oryctolagus cuniculus 184-192 7877603-1 1994 Cytochrome P450 LM2 (CYPIIB4) from phenobarbital-induced rabbit liver microsomes, purified to only one band in SDS-PAGE, was further resolved in five peaks by cation exchange HPLC. Phenobarbital 35-48 cytochrome P450 2B4 Oryctolagus cuniculus 0-19 7877603-1 1994 Cytochrome P450 LM2 (CYPIIB4) from phenobarbital-induced rabbit liver microsomes, purified to only one band in SDS-PAGE, was further resolved in five peaks by cation exchange HPLC. Phenobarbital 35-48 cytochrome P450 2B4 Oryctolagus cuniculus 21-28 2859164-1 1985 The possible role of free hydroxyl radicals in the oxidation of cyclohexanol to cyclohexanone and of benzene to phenol was examined in a reconstituted system containing rabbit phenobarbital-inducible P-450LM2. Phenobarbital 176-189 cytochrome P450 2B4 Oryctolagus cuniculus 200-208 3780743-7 1986 The rabbit enzyme metabolized the hydrocarbon with an apparent Vmax of 4 nmol nmol-1 min-1 and a Km of 8 microM, By contrast, phenobarbital-inducible P-450 LM2 or 3-methylcholanthrene-inducible P-450 LM4 from rabbit liver were quite ineffective catalysts of n-pentane metabolism. Phenobarbital 126-139 cytochrome P450 2B4 Oryctolagus cuniculus 150-203 2877820-2 1986 However, the increased rate of metabolism cannot be completely accounted for by the activity of the purified phenobarbital-inducible cytochrome P-450 isozyme 2, even in the presence of cytochrome b5. Phenobarbital 109-122 cytochrome P450 2B4 Oryctolagus cuniculus 133-159 2877820-3 1986 The discovery of a second hepatic phenobarbital-inducible cytochrome P-450, isozyme 5, led us to undertake experiments to determine in hepatic and pulmonary preparations the portion of microsomal metabolism of methoxyflurane catalyzed by cytochrome P-450 isozymes 2 and 5. Phenobarbital 34-47 cytochrome P450 2B4 Oryctolagus cuniculus 238-271 4041439-0 1985 Effects of detergent on substrate binding and spin state of purified liver microsomal cytochrome P-450LM2 from phenobarbital-treated rabbits. Phenobarbital 111-124 cytochrome P450 2B4 Oryctolagus cuniculus 86-105 4041439-1 1985 Spectral changes accompanying the binding of the nonionic detergent n-octyl beta-D-glucopyranoside (n-octyl glucoside) to cytochrome P-450LM2 purified from liver microsomes of phenobarbital-treated rabbits have been compared to changes in catalytic activity obtained in a reconstituted system consisting of various levels of detergent, P-450LM2, and NADPH-cytochrome P-450 reductase. Phenobarbital 176-189 cytochrome P450 2B4 Oryctolagus cuniculus 122-141 4041439-1 1985 Spectral changes accompanying the binding of the nonionic detergent n-octyl beta-D-glucopyranoside (n-octyl glucoside) to cytochrome P-450LM2 purified from liver microsomes of phenobarbital-treated rabbits have been compared to changes in catalytic activity obtained in a reconstituted system consisting of various levels of detergent, P-450LM2, and NADPH-cytochrome P-450 reductase. Phenobarbital 176-189 cytochrome P450 2B4 Oryctolagus cuniculus 133-141 3427076-5 1987 Similar isotope effects were reached with reconstituted membranes containing the rabbit ethanol-inducible cytochrome P-450 (LMeb), whereas control rat microsomes and membranes containing rabbit phenobarbital-inducible P-450 LM2 oxidized the alcohol with D(V/K) of about 2.8 and 1.8, respectively. Phenobarbital 194-207 cytochrome P450 2B4 Oryctolagus cuniculus 218-227 3113486-0 1987 Influence of N,N-dimethylaniline on the association of phenobarbital-induced cytochrome P-450 and NADPH-cytochrome c(P-450) reductase in a reconstituted rabbit liver microsomal enzyme system. Phenobarbital 55-68 cytochrome P450 2B4 Oryctolagus cuniculus 88-93 3113486-0 1987 Influence of N,N-dimethylaniline on the association of phenobarbital-induced cytochrome P-450 and NADPH-cytochrome c(P-450) reductase in a reconstituted rabbit liver microsomal enzyme system. Phenobarbital 55-68 cytochrome P450 2B4 Oryctolagus cuniculus 117-122 3113486-1 1987 N,N-Dimethylaniline when added to reaction mixtures provokes deviation from Michaelis-Menten law of the interaction kinetics of NADPH-cytochrome c(P-450) reductase (NADPH:ferrihaemoprotein oxidoreductase, EC 1.6.2.4) with highly purified phenobarbital-induced rabbit liver microsomal cytochrome P-450 (P-450LM2). Phenobarbital 238-251 cytochrome P450 2B4 Oryctolagus cuniculus 147-152 3113479-11 1987 An apparent correlation between P-450 aggregation state and NADPH-supported hydroxylation was also observed with phenobarbital-inducible P-450LM2 in the presence of detergents [Dean, W.L., & Gray, R.D. Phenobarbital 113-126 cytochrome P450 2B4 Oryctolagus cuniculus 137-145 2877820-6 1986 In summary, we demonstrate that methoxyflurane O-demethylation in lung, phenobarbital-induced liver, and control liver microsomes is catalyzed by cytochrome P-450 isozymes 2 and 5. Phenobarbital 72-85 cytochrome P450 2B4 Oryctolagus cuniculus 146-179 3967237-5 1985 Cytochrome P-450LM2, which is induced by pretreatment with phenobarbital, exhibited the highest activity for the metabolism of cis-NNDM. Phenobarbital 59-72 cytochrome P450 2B4 Oryctolagus cuniculus 0-19 6589592-7 1984 Comparison with phenobarbital-induced rabbit cytochrome P-450 isozyme 2 indicated about 25% homology. Phenobarbital 16-29 cytochrome P450 2B4 Oryctolagus cuniculus 45-71 6421810-1 1984 The zwitterionic detergent 3-(3-cholamidopropyl)-dimethylammonio-1-propanesulfonate (CHAPS) supports reconstituted cyclohexane hydroxylase activity of cytochrome P-450LM2 and NADPH-cytochrome reductase purified from phenobarbital-induced rabbit liver. Phenobarbital 216-229 cytochrome P450 2B4 Oryctolagus cuniculus 151-170 6722175-2 1984 Phenobarbital-inducible isozyme cytochrome P-450 LM2 (RH, reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating), EC 1.14.14.1) from rabbit liver microsomes has been modified with N-acetylimidazole and tetranitromethane. Phenobarbital 0-13 cytochrome P450 2B4 Oryctolagus cuniculus 32-52 7174657-3 1982 However, our present studies on the primary structure of the phenobarbital-inducible cytochrome from rabbit liver microsomes (P-450LM2) show that this protein is about 80% identical to the corresponding rat protein (P-450b), the sequence of which was recently deduced by others. Phenobarbital 61-74 cytochrome P450 2B4 Oryctolagus cuniculus 126-134 6579541-0 1983 Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. Phenobarbital 64-77 cytochrome P450 2B4 Oryctolagus cuniculus 86-113 6579541-1 1983 The complete amino acid sequence of phenobarbital-induced isozyme 2 of rabbit liver microsomal cytochrome P-450 (P-450LM2) is presented. Phenobarbital 36-49 cytochrome P450 2B4 Oryctolagus cuniculus 58-67 6579541-1 1983 The complete amino acid sequence of phenobarbital-induced isozyme 2 of rabbit liver microsomal cytochrome P-450 (P-450LM2) is presented. Phenobarbital 36-49 cytochrome P450 2B4 Oryctolagus cuniculus 106-111 6579541-1 1983 The complete amino acid sequence of phenobarbital-induced isozyme 2 of rabbit liver microsomal cytochrome P-450 (P-450LM2) is presented. Phenobarbital 36-49 cytochrome P450 2B4 Oryctolagus cuniculus 113-121 6833251-0 1983 The complete amino acid sequence of rabbit phenobarbital-induced liver microsomal cytochrome P-450. Phenobarbital 43-56 cytochrome P450 2B4 Oryctolagus cuniculus 93-98 6833251-1 1983 The complete amino acid sequence of the major phenobarbital-induced cytochrome P-450 (P-450LM2) from rabbit liver microsomes has been determined. Phenobarbital 46-59 cytochrome P450 2B4 Oryctolagus cuniculus 79-84 6833251-1 1983 The complete amino acid sequence of the major phenobarbital-induced cytochrome P-450 (P-450LM2) from rabbit liver microsomes has been determined. Phenobarbital 46-59 cytochrome P450 2B4 Oryctolagus cuniculus 86-94 7109711-0 1982 The quantitation of liver cytochrome P450-LM2 mRNA in rabbits of different ages and after phenobarbital treatment. Phenobarbital 90-103 cytochrome P450 2B4 Oryctolagus cuniculus 26-45 7109711-4 1982 Using a specific assay for translatable cytochrome P450-LM2 mRNA, we show that the age-dependent decrease in control and phenobarbital-induced enzyme activities is due to a decrease in the levels of translatable mRNA specific for cytochrome P450-LM2. Phenobarbital 121-134 cytochrome P450 2B4 Oryctolagus cuniculus 40-59 7109711-4 1982 Using a specific assay for translatable cytochrome P450-LM2 mRNA, we show that the age-dependent decrease in control and phenobarbital-induced enzyme activities is due to a decrease in the levels of translatable mRNA specific for cytochrome P450-LM2. Phenobarbital 121-134 cytochrome P450 2B4 Oryctolagus cuniculus 230-249 1123353-5 1975 P-450LM2, which was purified to apparent homogeneity, is induced by phenobarbital and has a subunit molecular weight of 50,000. Phenobarbital 68-81 cytochrome P450 2B4 Oryctolagus cuniculus 0-8 7213733-1 1981 We demonstrate the in vitro synthesis of cytochrome P-450-LM2 (phenobarbital-inducible form of liver microsomal cytochrome P-450) from a rabbit liver polysomal mRNA template by specific immunoprecipitation of the product. Phenobarbital 63-76 cytochrome P450 2B4 Oryctolagus cuniculus 41-61 7213733-3 1981 In addition, we demonstrate that phenobarbital increases the amount of translatable mRNA for cytochrome P-450-LM2 but not for albumin, suggesting that phenobarbital has selective effects on the amount of available translatable mRNA or on mRNA biosynthesis. Phenobarbital 33-46 cytochrome P450 2B4 Oryctolagus cuniculus 93-113 7213733-3 1981 In addition, we demonstrate that phenobarbital increases the amount of translatable mRNA for cytochrome P-450-LM2 but not for albumin, suggesting that phenobarbital has selective effects on the amount of available translatable mRNA or on mRNA biosynthesis. Phenobarbital 151-164 cytochrome P450 2B4 Oryctolagus cuniculus 93-113 187601-3 1976 P-450LM2, which was isolated from phenobarbital-induced animals, has a subunit molecular weight of 48,700. Phenobarbital 34-47 cytochrome P450 2B4 Oryctolagus cuniculus 0-8 7061465-5 1982 Two isozymes of rabbit liver microsomal cytochrome P-450 were examined: the isozyme induced by phenobarbital (P-450LM2), which has a sixth ligand and is low spin and the isozyme induced by 5,6-benzoflavone (P-450LM4), which is without a sixth ligand and is high spin. Phenobarbital 95-108 cytochrome P450 2B4 Oryctolagus cuniculus 110-118