Academic literature on the topic 'Cytochrome P-450'

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Journal articles on the topic "Cytochrome P-450"

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Izotov, MV, VM Shcherbakov, VM Devichensky, SM Spiridonova, LV Lugovaja, and SA Benediktova. "The ratio of two isozyme groups in microsomal cytochrome P‐450 under exogenous influence of carbon tetrachloride and cyclophosphamide." Biotechnology and Applied Biochemistry 10, no. 6 (December 1988): 545–50. http://dx.doi.org/10.1111/j.1470-8744.1988.tb00042.x.

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A method for measuring the content of two groups of microsomal cytochrome P‐450 isozymes–cytochromes P‐450W and P‐450L–with the active sites directed into the water phase and membrane lipids, respectively, has been developed. The method is based on the ability of the xanthine oxidase‐menadione complex to reduce microsomal cytochromes b5 and P‐450 under anaerobic conditions by transferring electrons to hemoproteins with the active sites directed into the water phase. Cytochrome b5 is completely reduced (to the dithionite level) and cytochrome P‐450 is reduced partially (only a group of cytochromes P‐450W). The amount of cytochromes P‐450L is estimated using the difference between the total content of cytochrome P‐450 reduced by sodium dithionite and the content of cytochromes P‐450W. The possibility of controlling the ratio of these two isozyme groups in cytochrome P‐450 in vivo in membranes of the endoplasmic reticulum by pretreatment of animals with a variety of chemicals has been demonstrated. The ratio of cytochromes P‐450W and P‐450L has been shown to decrease two‐fold 18 days after three injections of phenobarbital into mice. Carbon tetrachloride and cyclophosphamide also decrease this ratio in vivo.
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WHITE, R. E. "Cytochrome P-450: Cytochrome P-450." Science 234, no. 4778 (November 14, 1986): 884. http://dx.doi.org/10.1126/science.234.4778.884.

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Kapitulnik, J., J. P. Hardwick, J. D. Ostrow, C. C. Webster, S. S. Park, and H. V. Gelboin. "Increase in a specific cytochrome P-450 isoenzyme in the liver of congenitally jaundiced Gunn rats." Biochemical Journal 242, no. 1 (February 15, 1987): 297–300. http://dx.doi.org/10.1042/bj2420297.

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Congenitally jaundiced (jj) Gunn rats had a greater hepatic microsomal content of a cytochrome P-450 isoenzyme, P-450c, than did the non-jaundiced (Jj) rats. No differences in content of P-450b, P-450d and pregnenolone-16 alpha-carbonitrile-induced (PCN) P-450 were found between jj and Jj rats. This is the first demonstration of a constitutive increase in a specific cytochrome P-450 isoenzyme in association with a genetic defect.
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Strobel, Henry W., Steven G. Nadler, and David R. Nelson. "Cytochrome P-450: Cytochrome P-450 Reductase Interactions." Drug Metabolism Reviews 20, no. 2-4 (January 1989): 519–33. http://dx.doi.org/10.3109/03602538909103558.

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Pessayre, D. "Cytochrome P 450." La Revue de Médecine Interne 10, no. 1 (January 1989): 23–24. http://dx.doi.org/10.1016/s0248-8663(89)80108-0.

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Pompon, D., and P. Urban. "Cytochrome P-450." Biochimie 76, no. 1 (January 1994): 89. http://dx.doi.org/10.1016/0300-9084(94)90068-x.

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Jacobs, J. M., P. R. Sinclair, W. J. Bement, R. W. Lambrecht, J. F. Sinclair, and J. A. Goldstein. "Oxidation of uroporphyrinogen by methylcholanthrene-induced cytochrome P-450. Essential role of cytochrome P-450d." Biochemical Journal 258, no. 1 (February 15, 1989): 247–53. http://dx.doi.org/10.1042/bj2580247.

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We have previously shown that uroporphyrinogen is oxidized to uroporphyrin by microsomes (microsomal fractions) from 3-methylcholanthrene-pretreated chick embryo liver [Sinclair, Lambrecht & Sinclair (1987) Biochem. Biophys. Res. Commun. 146, 1324-1329]. We report here that a specific antibody to chick liver methylcholanthrene-induced cytochrome P-450 (P-450) inhibited both uroporphyrinogen oxidation and ethoxyresorufin O-de-ethylation in chick-embryo liver microsomes. 3-Methylcholanthrene-pretreatment of rats and mice markedly increased uroporphyrinogen oxidation in hepatic microsomes as well as P-450-mediated ethoxyresorufin de-ethylation. In rodent microsomes, uroporphyrinogen oxidation required the addition of NADPH, whereas chick liver microsomes required both NADPH and 3,3',4,4'-tetrachlorobiphenyl. Treatment of rats with methylcholanthrene, hexachlorobenzene and o-aminoazotoluene increased uroporphyrinogen oxidation and P-450d, whereas phenobarbital did not increase either. The contribution of hepatic P-450c and P-450d to uroporphyrinogen oxidation and ethoxyresorufin O-de-ethylation in methylcholanthrene-induced microsomes was assessed by using specific antibodies to P-450c and P-450d. Uroporphyrinogen oxidation by methylcholanthrene-induced rat liver microsomes was inhibited up to 75% by specific antibodies to P-450d, but not by specific antibodies to P-450c. In contrast, ethoxyresorufin de-ethylation was inhibited only 20% by anti-P450d but 70% by anti-P450c. Methylcholanthrene-induced kidney microsomes which contain P-450c but non P-450d did not oxidize uroporphyrinogen. These data indicate that hepatic P-450d catalyses uroporphyrinogen oxidation. We suggest that the P-450d-catalysed oxidation of uroporphyrinogen has a role in the uroporphyria caused by hexachlorobenzene and other compounds.
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Reed, C. J., E. A. Lock, and F. De Matteis. "NADPH: cytochrome P-450 reductase in olfactory epithelium Relevance to cytochrome P-450-dependent reactions." Biochemical Journal 240, no. 2 (December 1, 1986): 585–92. http://dx.doi.org/10.1042/bj2400585.

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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 olfactory microsomes has been examined. By this criterion there was no evidence for marked differences in the spin state of the cytochromes of the two tissues, or for the olfactory epithelium containing a greater amount of cytochrome capable of binding hexobarbitone, a very actively metabolized substrate. Rates of NADPH and NADH: cytochrome c reductase activity were found to be higher in the olfactory epithelium than in the liver, and direct evidence was obtained for a greater amount of the NADPH-dependent flavoprotein in the olfactory microsomes. Investigation of male rats and male and female mice, as well as male hamsters, demonstrated that, in all cases, the cytochrome P-450 levels of the olfactory epithelium were lower than those of the liver, while the 7-ethoxycoumarin de-ethylase and NADPH:cytochrome c reductase activities were higher. A correlation was found between 7-ethoxycoumarin de-ethylase and NADPH:cytochrome c reductase activities for both tissues in all species examined. The ratio of reductase to cytochrome P-450 was found to be considerably higher in the olfactory epithelium (1:2-1:3) than in the liver (1:11-1:15), regardless of the species examined, suggesting that facilitated electron flow may contribute significantly to the cytochrome P-450 catalytic turnover in the olfactory tissue.
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Sinclair, J. F., S. Wood, L. Lambrecht, N. Gorman, L. Mende-Mueller, L. Smith, J. Hunt, and P. Sinclair. "Isolation of four forms of acetone-induced cytochrome P-450 in chicken liver by h.p.l.c. and their enzymic characterization." Biochemical Journal 269, no. 1 (July 1, 1990): 85–91. http://dx.doi.org/10.1042/bj2690085.

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The purpose of this study was to purify and characterize the forms of cytochrome P-450 induced in chicken liver by acetone or ethanol. Using high performance liquid ion-exchange chromatography, we were able to isolate at least four different forms of cytochrome P-450 which were induced by acetone in chicken liver. All four forms of cytochrome P-450 proved to be distinct proteins, as indicated by their N-terminal amino acid sequences and their reconstituted catalytic activities. Two of these forms, also induced by glutethimide in chicken embryo liver, appeared to be cytochromes P450IIH1 and P450IIH2. Both of these cytochromes P-450 have identical catalytic activities towards benzphetamine demethylation. However, they differ in their abilities to hydroxylate p-nitrophenol and to convert acetaminophen into a metabolite that forms a covalent adduct with glutathione at the 3-position. Another form of cytochrome P-450 induced by acetone is highly active in the hydroxylation of p-nitrophenol and in the conversion of acetaminophen to a reactive metabolite, similar to reactions catalysed by mammalian cytochrome P450IIE. Yet the N-terminal amino acid sequence of this form has only 30-33% similarity with cytochrome P450IIE purified from rat, rabbit and human livers. A fourth form of cytochrome P-450 was identified whose N-terminal amino acid sequence and enzymic activities do not correspond to any mammalian cytochromes P-450 reported to be induced by acetone or ethanol.
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Song, B. J., H. V. Gelboin, S. S. Park, and F. K. Friedman. "Epitope-relatedness and phenotyping of hepatic cytochromes P-450 with monoclonal antibodies." Biochemical Journal 231, no. 3 (November 1, 1985): 671–76. http://dx.doi.org/10.1042/bj2310671.

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The epitope-specific cytochrome P-450 content of animal livers was analysed by radioimmunoassay using a panel of seven monoclonal antibodies (MAbs) made to a 3-methylcholanthrene-induced rat liver cytochrome P-450. Competitive radioimmunoassays utilizing a reference radiolabelled MAb and a series of unlabelled MAbs indicated that there are at least three distinct classes of MAbs to different epitopes on cytochrome P-450. In addition, a direct radioimmunoassay employing a radiolabelled second antibody detected MAb-specific cytochromes P-450 in livers from different animals. This radioimmunoassay detected large elevations in the levels of these cytochromes P-450 in the livers of 3-methylcholanthrene-treated rats and C57BL/6 mice compared with untreated rats, 3-methylcholanthrene-treated DBA/2 mice or guinea pigs. The two complementary radioimmunoassay methods are sensitive, efficient, and easily applicable for screening large number of tissue samples for MAb-defined cytochrome P-450 phenotype.
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Dissertations / Theses on the topic "Cytochrome P-450"

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Clarke, Stephen Edward. "Characterisation of housefly cytochrome P-450." Thesis, University of Surrey, 1989. http://epubs.surrey.ac.uk/847312/.

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The cytochrome P-450 dependent monooxygenase activity in a 'wild type' susceptible strain of housefly was studied. Catalytic activities were identified that demonstrated that the housefly cytochrome P-450 was capable of similar catalytic functions as those described for higher animals. Although several specific activities were lower than in mammalian species, benzphetamine N-demethylation was comparable and there was higher constitutive activity toward lauric acid than is observed in rat hepatic microsomes. The inducing agent phenobarbital increased both total cytochrome P-450 content and the benzphetamine N-demethylase specific activity. The high constitutive activity for fatty acids was induced by the hypolipidaemic drug clofibrate, specifically inducing the w-hydroxylase activity. The substrate specificity toward lauric acid extended equally to myristic and palmitic acid. Housefly microsomal cytochrome P-450 also metabolised the unsaturated fatty acid, arachidonic acid, the w-hydroxy-lation again inducible by clofibrate pretreatment. The w-hydroxylation of these fatty acids appeared to be a well-coupled reaction, a property that also appeared to be exhibited by the rat hepatic w-hydroxylase. The housefly fatty acid hydroxylation showed certain similarities to that in the rat, both in the specificity for w-hydroxylation and in the result of induction by clofibrate. Structural comparison to cytochrome P-450IVA1, IIB1 and IA1 was made by Western blot analysis with polyclonal antibodies raised to these rat hepatic isoenzymes. Housefly cytochrome P-450 shared few, if any, common epitopes with these rat isoenzymes, nor did these antibodies inhibit housefly cytochrome P-450 dependent monooxygenase activity. Cytochrome P-450 from clofibrate-pretreated housefly microsomes was partially purified by affinity chromatography. The cytochrome P-450 had a specific content of 5. 7nmol.mg-1 and a monomeric molecular weight of 52,000 daltons and a reduced carbon monoxide difference spectrum absorbance maxima at 448nm. In a reconstituted system, this preparation exhibited activity toward lauric acid and to a lesser extent arachidonic acid in each case w-hydroxylated products predominated. This is the first example of a purification of an insect cytochrome P-450 multiple form with a defined product reaction.
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Jones, Barry Christopher. "Cytochrome P-450 mediated N-dealkylation." Thesis, University of Surrey, 1989. http://epubs.surrey.ac.uk/844436/.

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An investigation into the physico-chemical and molecular mechanical properties of tertiary amines which predispose them to rapid metabolism by cytochrome P-450 has been undertaken. A series of tertiary amines based on the common 2-(2,4-dichlorophenoxy)-N-methylethanamine moiety was synthesised with different substituent groups which changed the lipophilicity, size, polarity and electronic configuration. The substituent groups employed included n-alkyl, branched alkyl, aromatic, unsaturated, and oxygenated moieties. The design of the molecules was centred around an N~methyl group which was shown to be the major site of metabolism in a selected series of the molecules. The rates of N-demethylation were used as the index by which the effect of changing the substituent group was assessed. Studies using chemical inducers and inhibitors of cytochrome P-450 indicated that the hepatic microsomal fraction obtained from rats that had been pretreated with phenobarbital was the most effective biological system for the study of the rate of metabolism of these compounds. Further investigations using purified cytochrome P450 IIB4 in a reconstituted system showed that this particular isozyme of cytochrome P-450 was capable of supporting the metabolism of these compounds indicating that in the rat hepatic microsomes it was cytochrome P450 IIB1 which was mediating the compounds' metabolism. Various physico-chemical properties including lipophilicity, pKa and the octanol/water partition coefficient at pH 7.4 (log D) were determined for each of the compounds. The X-ray crystal structures of two of the molecules were solved to provide co-ordinates that were used in the determination of various molecular mechanical parameters such as the partial charges on the atoms in the molecules. The physico-chemical parameters were correlated with biological parameters obtained from both hepatic microsomal and purified cytochrome P450 IIB4 in a reconstituted system. The biological parameters determined were the binding affinity (K3, K3 and K4), the substrate-induced cytochrome P-450 spin state change (% HS and K2), Vmax and Km. No correlation was found between these parameters derived from the different biological systems. This may have been a result of changes in the tertiary structure of the enzyme brought about- as a result of the purification process or it may have been due to differences in the primary structures of cytochrome P450 IIB1 and IIB4. Quantitative structure-activity relationships derived between these sets of parameters for the microsomal system indicated that increasing size and lipophilicity produced stronger binding of the substrate to the enzyme, however, this gave no information about the orientation of the molecule in the enzyme's active site. A correlation was found for Km which indicated that the electronic structure of the molecules may influence the orientation that the molecule adopts in the active site of the enzyme. No correlations were found for Vmax, however the ratioVmax/Km produced a number of correlations which indicated that this parameter was dependent on the electron density on the nitrogen atom and the electronic influence of the substituent group on the nitrogen atom. Very few correlations were found for the biological parameters determined using purified cytochrome P450 IIB4 in a reconstituted system. Those that were obtained went a little way in supporting the suggestion that compounds bind to cytochrome P-450 via a hydrophobic interaction.
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Boitrel, Bernard. "Modeles d'hemoproteines : hemoglobine et cytochrome p-450." Paris 6, 1989. http://www.theses.fr/1989PA066059.

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Krause, Maren. "Genetische Variabilität des Cytochrom P 450- Systems im Zusammenhang mit einem erhöhten Risiko für Rheumatoide Arthritis." Doctoral thesis, Universitätsbibliothek Leipzig, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-143774.

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Rheumatoid Arthritis is a chronic inflammatory systemic disease and is one of the autoimmune diseases. In this study, nine candidate genes of the cytochrome P450 system have been analyzed to determine their possible association with the formation of RA. These genes are: CYP1A1, CYP1B1, CYP2B6, CYP2E1, CYP2C9, CYP2D6, CYP2A6, CYP2C19 and CYP3A4.Within these genes, 21 single nucleotide polymorphism, SNPs, in 300 French Caucasian individuals (100 RA trio families) were genotyped using single-base-extensions, SBE, in a mass spectrometric analysis by MALDI-TOF-MS (matrix-assisted Laser Desorption/ Ionization-time-of-flight mass spectometry). The selection of the examined genes was carried out taking into account known associations with RA or other autoimmune disease, as well as known functional variants. Decisive were also the location of the gene and genetic variability. The results of genotyping were used to study polymorphisms on their association with Rheumatoid Arthritis. The statistical analyzes of CYP2C9 rs1799853 (3011) showed, in the family-based single-marker test, a lower transmission (TDT p-value 0.021) for the rare allele (3011-a). The case-control allelic based test shows, there is a protective effect (Odds Ratio 0.58). In the case-control-based genotypic test this issue could be reproduced (p-value 0.046). For the rare allele of the CYP2A6 rs1801272 (3022-a) the family-based single-marker test shows a lower transmittance (TDT p-value 0.037). The case-control allelic based test shows a protective effect of this allele (Odds Ratio 0.32). In the case-control-based genotypic test a statistical trend to protective behavior of this allele occurs. SNPs with predicted functional relevance showed no statistical abnormalities in the studied cohort. In genome-wide studies, the results could not be tracked, at least at the gene level weak associations could be detected. The results of this study should be to replicate in one second independent cohort. Care should be taken specifically to xenobiotic stress, such as job stress, smoking, and medication. In subsequent studies more SNPs of the candidate genes could also genotyped in order to verify the genetic variability with reference to of the haplotypes in more detail. Should the above-mentioned associations be confirmed, functional studies on different gene expression or altered metabolite spectrum are highly interesting.
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Chassagne, Philippe. "Expression des cytochromes P-450 pancréatiques." Montpellier 1, 1994. http://www.theses.fr/1994MON11135.

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Zhao, Jin 1975. "Investigations of the biocatalytic activity of human P450 2D6." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111940.

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The cytochrome P450 enzymes (CYPs) are very attractive biocatalysts because of their ability to regio- and stereo-selectively catalyze the insertion of a single atom of molecular oxygen into inactivated C-H bonds. There are many drawbacks, however, limiting the use of these enzymes in organic synthesis, including the need for expensive cofactors, low stability, and low tolerance to organic solvents. The goal of this thesis was to overcome some of these drawbacks for human CYP2D6. This isoform was selected because of its broad substrate promiscuity and high importance in drug metabolism.
We have tested inexpensive chemicals to replace the natural cofactors of CYP2D6, NADPH and cytochrome P450 reductase (CPR). The results showed that cumene hydroperoxide and tert-butyl hydroperoxide can successfully substitute CPR and NAD(P)H with retained regio- and stereo-selectivity. Moreover, with these surrogates, product formation and initial rates are increased by as much as two fold compared to the use of the natural cofactors.
It is widely accepted that even small proportions of organic solvents in the buffer can deactivate most enzymes including P450s. Our studies on the biocatalysis of CYP2D6 in organic solvent/buffer emulsions showed that under the optimized conditions, as much as 76% of the enzyme activity was retained. Product formation in biphasic solvent systems is comparable whether the natural redox partner and cofactor are used, or a surrogate. In addition, a correlation was observed between the log P and the suitability of a solvent for enzymatic activity, with higher log P resulting in higher enzymatic activity. These results were obtained with dextromethorphan (DXM), a water soluble substrate. A very hydrophobic substrate, 7-benzyloxy-4-N,N-diethylaminomethyl-coumarin (BDAC), was also tested successfully to demonstrate the utility of this method.
Lyophilization is usually required to remove water before using enzymes in nearly anhydrous solvents. This physical process is harmful to P450 enzyme activity. We therefore tested numerous sugars as lyoprotectant during lyophilization. Addition of trehalose or sucrose before lyophilization allowed the retention of 80% of the CYP2D6 activity, compared to 40% remaining activity in its absence. CYP2D6 co-lyophilized with trehalose was next tested in selected hydrophobic organic solvents in the absence of water. The enzymatic activity was found to strongly depend on the hydrophobicity of the solvent. Interestingly, the enzyme showed higher catalytic ability in n-decane or n-dodecane than in the standard buffer. This was unexpected considering that the activity of most enzymes was reported to decrease to 10% or less in nearly anhydrous organic solvents.
The last objective of this thesis was to improve the stability and/or activity of CYP2D6. Use of DNA self-assemblies to encapsulate P450 enzymes was envisaged to potentially increase their stability. Indeed, DNA assemblies have many advantages compared to traditional solid supports reported for enzymes. Our preliminary results showed that CYP2D6 templated the formation of cyclic DNA dimeric and tetrameric over polymeric self-assemblies. Characterization of the CYP2D6 activity in the presence of the DNA self-assemblies revealed no loss of activity or stability.
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Rodrigues, N. R. "The human cytochrome P-450 21-hydroxylase genes." Thesis, University of Oxford, 1987. http://ora.ox.ac.uk/objects/uuid:77be8950-4675-4a55-ab4f-27b788082007.

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Deficiency of the cytochrome P-450 steroid 21-hydroxylase (21-OHase) which causes Congenital Adrenal Hyperplasia (CAH) is a monogenic autosomal recessive disorder which is linked to HLA. There are two 21-OHase genes in man, A and B, and they are mapped to the HLA class III region ~ 3 kb 3' to the complement genes C4A and C4B, respectively. Two genes encoding 21-OHase were isolated, characterized and sequenced. Both 21-OHase genes are ~ 3.3 kb in length and are split into 10 exons by nine introns. Comparison of the two genes showed that although they are highly conserved, there are three deleterious mutations in the 21-OHase A gene which cause frameshifts and introduce in phase premature termination codons. Thus the 21-OHase A gene is a pseudogene. Comparison of the 21-OHase B gene to the other cytochrome P-450 sequences revealed that although the cysteine-429 was conserved in 21-OHase, there is very little homology with other cytochrome P-450, indicating it belongs to a separate family of genes within the superfamily. Clear evidence of polymorphism in 21-OHase is apparent on comparison with other 21-OHase B sequences. There is a size polymorphism of 494 and 495 amino acids. The differing severities of 21-OHase deficiency in CAH may be due to allelic variants of the 21-OHase B gene, since in most cases the defect is not due to gene deletion (Rumsby et al., 1986). A 21-OHase B gene from a patient with CAH was characterized and sequenced. There were 13 nucleotide alterations in his single 21-OHase B gene, one of which at codon 269 caused a serine to change to a threonine residue. The G → C transversion in the 21-OHase B gene from the patient at codon 269 introduced a new NcoI restriction site into the gene. This restriction fragment length polymorphism (RFLP) was used to study other patients with CAH and normal individuals. The NcoI RFLP was found not to be confined to the 21-OHase B gene but was also present in some 21-OHase A genes. It is likely therefore that the mutation occurred in the pseudogene first and then transferred to some 21-OHase B genes.
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Slatcher, Guy. "The mechanistic enzymology of cytochrome P-450 aromatase." Thesis, University of Southampton, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.307085.

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Chow, Cathy Sze-Yu. "Selective hydroxylations catalysed by cytochrome P-450 monooxygenases." Thesis, University of Edinburgh, 1998. http://hdl.handle.net/1842/13386.

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The biohydroxylation potential of the mutant enzyme, cytochrome P-450 cam Y96A monooxygenase (Y96A), has been investigated with a series of substrates which differ structurally from that of the natural substrate, D-(+)-camphor. Design of substrates essentially consisted of coupling an aromatic side-chain with an alicyclic moiety via an ester, ether or amide link. Assays have been performed with Y96A in order to obtain data on key factors of the biohydroxylation reaction such as substrate binding and turnover to give hydroxylated products. Y96A research has been complemented by a thorough investigation of the biohydroxylation capability of bacterium, Rhodococcus rhodochrous NCIMB 9703. Compounds found to be inactive with Y96A were reacted with this whole cell system, and positive results have been achieved in all cases.
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Hawkes, David B. "Cytochrome P450cin /." St. Lucia, Qld, 2003. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe17457.pdf.

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Books on the topic "Cytochrome P-450"

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1930-, Omura Tsuneo, Ishimura Yuzuru 1935-, and Fujii-Kuriyama Yoshiaki, eds. Cytochrome P-450. 2nd ed. Tokyo: Kodansha, 1993.

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de Montellano, Paul R. Ortiz, ed. Cytochrome P-450. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2.

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Emel, Arinç, Schenkman John B, and Greim Helmut, eds. Cytochrome P450. Berlin: Springer-Verlag, 1993.

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Paul R. Ortiz de Montellano, Ian R. Phillips, and Elizabeth A. Shephard. Cytochrome P450 protocols. 3rd ed. New York: Humana, 2013.

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Ortiz de Montellano, Paul R., ed. Cytochrome P-450: Structure, mechanism, and biochemistry. New York: Plenum Press, 1986.

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1951-, Phillips Ian R., and Shephard Elizabeth A. 1950-, eds. Cytochrome P450 protocols. 2nd ed. Totowa, N.J: Humana Press, 2005.

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R, Waterman Michael, and Johnson Eric F, eds. Cytochrome P450. San Diego: Academic Press, 1991.

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Peter, Guengerich F., ed. Mammalian cytochromes P-450. Boca Raton, FL: CRC Press, 1987.

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Ortiz de Montellano, Paul R., ed. Cytochrome P-450: Structure, mechanismand biochemistry. New York: Plenum, 1986.

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1946-, Bachmanova G. I., ed. Cytochrome P-450 and active oxygen. London: Taylor & Francis, 1990.

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Book chapters on the topic "Cytochrome P-450"

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Peterson, Julian A., and Russell A. Prough. "Cytochrome P-450 Reductase and Cytochrome b5 in Cytochrome P-450 Catalysis." In Cytochrome P-450, 89–117. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_4.

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Sligar, Stephen G., and Ralph I. Murray. "Cytochrome P-450cam and Other Bacterial P-450 Enzymes." In Cytochrome P-450, 429–503. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_12.

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McMurry, Thomas J., and John T. Groves. "Metalloporphyrin Models for Cytochrome P-450." In Cytochrome P-450, 1–28. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_1.

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Waterman, Michael R., Maliyakal E. John, and Evan R. Simpson. "Regulation of Synthesis and Activity of Cytochrome P-450 Enzymes in Physiological Pathways." In Cytochrome P-450, 345–86. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_10.

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Jefcoate, Colin R. "Cytochrome P-450 Enzymes in Sterol Biosynthesis and Metabolism." In Cytochrome P-450, 387–428. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_11.

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6

Poulos, Thomas L. "The Crystal Structure of Cytochrome P-450cam." In Cytochrome P-450, 505–23. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_13.

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Marnett, Lawrence J., Paul Weller, and John R. Battista. "Comparison of the Peroxidase Activity of Hemeproteins and Cytochrome P-450." In Cytochrome P-450, 29–76. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_2.

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Miwa, Gerald T., and Anthony Y. H. Lu. "The Topology of the Mammalian Cytochrome P-450 Active Site." In Cytochrome P-450, 77–88. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_3.

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Ingelman-Sundberg, Magnus. "Cytochrome P-450 Organization and Membrane Interactions." In Cytochrome P-450, 119–60. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_5.

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Black, Shaun D., and Minor J. Coon. "Comparative Structures of P-450 Cytochromes." In Cytochrome P-450, 161–216. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-9939-2_6.

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Conference papers on the topic "Cytochrome P-450"

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D’yachkov, P. N. "Quantum chemical simulation of the cytochrome P 450 catalyzed oxidation and toxicity of benzene derivatives." In The first European conference on computational chemistry (E.C.C.C.1). AIP, 1995. http://dx.doi.org/10.1063/1.47657.

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Dervisis, Nikolaos G., Maciej Parys, Annet Wenker, Patrick Venta, Barbara E. Kitchell, and Vilma Yuzbasiyan-Gurkan. "Abstract 2661: Evaluation of genetic variability of cytochrome P-450 members in the canine preclinical model." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2661.

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Fenile, R., A. Nazário, and G. Facina. "P5-05-07: The Msp1 Polymorphism of Cytochrome P-450 CYP1A1 in Asymptomatic Women with Breast Cysts." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p5-05-07.

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Marcus, A. J., L. B. Safier, H. L. Ullman, N. Islam, M. J. Broekman, and C. V. Schacky. "NEW EICOSANOIDS FORMED DURING PLATELET-NEUTROPHIL INTERACTIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644626.

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Abstract:
In physiologic and pathologic processes such as hemostasis, thrombosis and inflammation, multiple cell types are brought into close proximity - thereby increasing the possibility of metabolic interactions in the microenvironment. Activated platelets synthesize12-hydroxyeicosatetraenoic acid (12-HETE) in the presence or absence of aspirin. During a cell-cell interaction, platelet 12-HETE is metabolized by a cytochrome P-450 enzyme system in unstimulated neutrophils to 12.20-dihydroxyeicosatetraenoic acid (12,20-DiHETE). Recently, we observed time-dependent formation of a new eicosanoid following exposure of neutrophils to 12-HETE. This compound is more polar than the parent eicosanoid 12,20-DiHETE (reversed-phase HPLC). Incubation of purified 12,20-DiHETE with neutrophils resulted in a progressive decrease in the 12,20-DiHETE with increasing formation of the polar metabolite. In the absence of neutrophils, 12.20-DiHETE was quantitatively unchanged. The new metabolite of 12.20-DiHETE has been tentatively identified as 12-hydroxyeicosatetraen-l,20-dioic acid. The UV absorption maximum of the new compound is 237 nm which is identical to that of 12-HETE and 12,20-DiHETE. 20-hydroxy-LTB4 is the omega-hydroxylated derivative of the pro-inflammatory eicosanoid LTB4. When added to neutrophils 15 sec prior to 12,20-DiHETE, equimolar concentrations of 20-hydroxy-LTB4 (2.8uM) inhibited formation of the new metabolite by 28%. A concentration of 8uM 20-hydroxy-LTB4 inhibited the reaction by 49%. These results indicate that the neutrophil enzyme system responsible for conversion of 20-hydroxy-LTB4 to 20-carboxy-LTB4 may also be involved in further metabolism of-12,20-DiHETE. Neutrophil homogenization resulted in loss of the capacity to transform 12.20-DiHETE to the new metabolite despite pretreatment with DFP and addition of NADPH. Our data provide further evidence for the occurrence of transcellular metabolic events during thrombosis and the inflammatory response.
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Reports on the topic "Cytochrome P-450"

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Carpenter, Hillary M., and Lawrence R. Curtis. Pharmacokinetics of Lipophilic Agents Following Preexposure: Non-Cytochrome P-450 Mediated Mechanisms. Fort Belvoir, VA: Defense Technical Information Center, May 1990. http://dx.doi.org/10.21236/ada225356.

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