Log in

Relevant bibliographies by topics / Cytochrome P-450 / Journal articles

To see the other types of publications on this topic, follow the link: Cytochrome P-450.

Journal articles on the topic 'Cytochrome P-450'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Cytochrome P-450.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

11

Mukhtar, Hasan, and Wasiuddin A. Khan. "Cutaneous Cytochrome P-450." Drug Metabolism Reviews 20, no. 2-4 (January 1989): 657–73. http://dx.doi.org/10.3109/03602538909103568.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

YASUKOCHI, Takanori, Hideo KOGA, Yasuhiro SAGARA, and Tadao HORIUCHI. "Bacterial Cytochrome P-450." Journal of the agricultural chemical society of Japan 66, no. 2 (1992): 145–48. http://dx.doi.org/10.1271/nogeikagaku1924.66.145.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Lee, Richard F. "Annelid cytochrome P-450." Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology 121, no. 1-3 (November 1998): 173–79. http://dx.doi.org/10.1016/s0742-8413(98)10037-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Bergman, T., and H. Postlind. "Characterization of mitochondrial cytochromes P-450 from pig kidney and liver catalysing 26-hydroxylation of 25-hydroxyvitamin D3 and C27 steroids." Biochemical Journal 276, no. 2 (June 1, 1991): 427–32. http://dx.doi.org/10.1042/bj2760427.

Full text

Abstract:

The properties of cytochrome P-450 from pig kidney mitochondria, catalysing 26-hydroxylation of 25-hydroxyvitamin D3 and C27 steroids [Postlind & Wikvall (1989) Biochem. Biophys. Res. Commun. 159, 1135-1140; Postlind (1990) Biochem. Biophys. Res. Commun. 168, 261-266], were compared with those of a 26-hydroxylating cytochrome P-450 from pig liver mitochondria. The liver enzyme was purified to a cytochrome P-450 content of 7.4 nmol/mg of protein and showed only one protein band with an apparent Mr of 53,000 upon SDS/PAGE. The cytochrome P-450 catalysed 26-hydroxylation of 25-hydroxyvitamin D3, cholesterol and 5 beta-cholestane-3 alpha, 7 alpha-diol at rates of 361, 1090 and 2065 pmol/min per nmol of cytochrome P-450. A monoclonal antibody against the purified liver mitochondrial cytochrome P-450 26-hydroxylase (cytochrome P-450(26] was prepared. After coupling to Sepharose, the antibody was able to bind to cytochrome P-450(26) from liver as well as from kidney mitochondria and to immunoprecipitate the 26-hydroxylase activity towards 25-hydroxyvitamin D3 and cholesterol when assayed in a reconstituted system. After SDS/PAGE and immunoblotting with the antibody, the cytochrome P-450(26) was detected in the purified liver and kidney preparations. These results indicate that similar species of cytochrome P-450 catalyse 26-hydroxylation of 25-hydroxyvitamin D3 and C27 steroids in liver and kidney mitochondria. The results with the monoclonal antibody together with the finding that cholesterol competitively inhibits the 26-hydroxylation of 25-hydroxyvitamin D3 further indicate that 26-hydroxylation of 25-hydroxyvitamin D3 and cholesterol is catalysed by the same species of cytochrome P-450 in each tissue. The N-terminal amino acid sequence of cytochrome P-450(26) in kidney mitochondria resembled that of pig kidney microsomal 25-hydroxylase active in 25-hydroxylation of vitamin D3 and C27 steroids, whereas the sequence of pig liver mitochondrial cytochrome P-450(26) differed from those of rabbit and rat liver mitochondrial 26-hydroxylases as well as from those of other hitherto isolated mammalian cytochromes P-450.

APA, Harvard, Vancouver, ISO, and other styles

15

Bergman, T., and H. Postlind. "Characterization of pig kidney microsomal cytochrome P-450 catalysing 25-hydroxylation of vitamin D3 and C27 steroids." Biochemical Journal 270, no. 2 (September 1, 1990): 345–50. http://dx.doi.org/10.1042/bj2700345.

Full text

Abstract:

The cytochrome P-450 enzyme which catalyses 25-hydroxylation of vitamin D3 (cytochrome P-450(25] from pig kidney microsomes [Postlind & Wikvall (1988) Biochem. J. 253, 549-552] has been further purified. The specific content of cytochrome P-450 was 15.0 nmol.mg of protein-1, and the protein showed a single spot with an apparent isoelectric point of 7.4 and an Mr of 50,500 upon two-dimensional isoelectric-focusing/SDS/PAGE. The 25-hydroxylase activity towards vitamin D3 was 124 pmol.min-1.nmol of cytochrome P-450-1 and towards 1 alpha-hydroxyvitamin D3 it was 1375 pmol.min-1.nmol-1. The preparation also catalysed the 25-hydroxylation of 5 beta-cholestane-3 alpha,7 alpha-diol at a rate of 1000 pmol.min-1.nmol of cytochrome P-450-1 and omega-1 hydroxylation of lauric acid at a rate of 200 pmol.min-1.nmol of cytochrome P-450-1. A monoclonal antibody raised against the 25-hydroxylating cytochrome P-450, designated mAb 25E5, was prepared. After coupling to Sepharose, the antibody was able to bind to cytochrome P-450(25) from kidney as well as from pig liver microsomes, and to immunoprecipitate the activity for 25-hydroxylation of vitamin D3 and 5 beta-cholestane-3 alpha,7 alpha-diol when assayed in a reconstituted system. The hydroxylase activity towards lauric acid was not inhibited by the antibody. By SDS/PAGE and immunoblotting with mAb 25E5, cytochrome P-450(25) was detected in both pig kidney and pig liver microsomes. These results indicate a similar or the same species of cytochrome P-450 in pig kidney and liver microsomes catalysing 25-hydroxylation of vitamin D3 and C27 steroids. The N-terminal amino acid sequence of the purified cytochrome P-450(25) from pig kidney microsomes differed from those of hitherto isolated mammalian cytochromes P-450.

APA, Harvard, Vancouver, ISO, and other styles

16

Takemori, Shigeki. "Molecular focus on cytochrome P-450 cytochrome P-450: Structure, mechanism, and biochemistry." Trends in Biochemical Sciences 12 (January 1987): 118. http://dx.doi.org/10.1016/0968-0004(87)90053-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Watkins, Paul B., Scott A. Murray, Paul E. Thomas, and Steven A. Wrighton. "Distribution of cytochromes P-450, cytochrome b5, and nadph-cytochrome P-450 reductase in an entire human liver." Biochemical Pharmacology 39, no. 3 (February 1990): 471–76. http://dx.doi.org/10.1016/0006-2952(90)90052-m.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Nisimoto, Yukio, and Hidetsugu Otsuka-Murakami. "Cytochrome b5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles." Biochemistry 27, no. 16 (August 1988): 5869–76. http://dx.doi.org/10.1021/bi00416a008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

DAMON, Marie, Alain FAUTREL, André GUILLOUZO, and Laurent CORCOS. "Genetic analysis of the phenobarbital regulation of the cytochrome P-450 2b-9 and aldehyde dehydrogenase type 2 mRNAs in mouse liver." Biochemical Journal 317, no. 2 (July 15, 1996): 481–86. http://dx.doi.org/10.1042/bj3170481.

Full text

Abstract:

The aim of this study was to investigate the effect of the genetic background on the phenobarbital inducibility of cytochrome P-450 2b-9, cytochrome P-450 2b-10 and aldehyde dehydrogenase type 2 mRNAs in mice. We analysed the basal expression and the phenobarbital inducibility of both cytochrome P-450 mRNAs by semi-quantitative specific reverse transcription-PCR analyses in five inbred mouse strains (A/J, BALB/cByJ, C57BL/6J, DBA/2J and SWR/J). Male mice constitutively expressed cytochrome P-450 2b-9 and cytochrome P-450 2b-10 mRNAs, but a number of differences in their response to phenobarbital were observed. In all these mouse strains, phenobarbital induced cytochrome P-450 2b-10 mRNA whereas it could have either a positive or a negative effect on cytochrome P-450 2b-9 expression, depending on the strain and the sex of the mice. Specifically, phenobarbital increased cytochrome P-450 2b-9 expression in C57BL/6J males while it decreased it in DBA/2J mice. Interestingly, dexamethasone was able to mimic the phenobarbital effect on both cytochromes P-450 in these two strains. Aldehyde dehydrogenase type 2 mRNA was always induced by phenobarbital, except in the C57BL/6J strain. Genetic analysis revealed that the phenobarbital-inducible phenotype was either a semi-dominant or a recessive trait in F1 animals from a C57BL/6J×DBA/2J cross for the cytochrome P-450 2b-9 and the aldehyde dehydrogenase type 2 genes, respectively. This study suggests that the genetic basis for phenobarbital induction in mice depends on the target gene, and that more than one regulatory step would be involved in this response pathway.

APA, Harvard, Vancouver, ISO, and other styles

20

Voigt, Jeffrey M., F. Peter Guengerich, and Jeffrey Baron. "Localization of a cytochrome P-450 isozyme (cytochrome P-450 PB-B) and NADPH-cytochrome P-450 reductase in rat nasal mucosa." Cancer Letters 27, no. 3 (July 1985): 241–47. http://dx.doi.org/10.1016/0304-3835(85)90180-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Kemper, Byron, and Elzbieta Szczesna-Skorupa. "Cytochrome P-450 Membrane Signals." Drug Metabolism Reviews 20, no. 2-4 (January 1989): 811–20. http://dx.doi.org/10.3109/03602538909103580.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

TAKAGI, Masamichi. "Cytochrome P-450 of Microorganisms." Journal of the agricultural chemical society of Japan 66, no. 2 (1992): 143–44. http://dx.doi.org/10.1271/nogeikagaku1924.66.143.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

SERIZAWA, Nobufusa. "Cytochrome P-450 of Actinomycetes." Journal of the agricultural chemical society of Japan 66, no. 2 (1992): 149–53. http://dx.doi.org/10.1271/nogeikagaku1924.66.149.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Fleming, Ingrid. "Cytochrome P-450 Under Pressure." Circulation 111, no. 1 (January 4, 2005): 5–7. http://dx.doi.org/10.1161/01.cir.0000152695.11867.d8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Backes, W. L., and C. S. Eyer. "Cytochrome P-450 LM2 Reduction." Journal of Biological Chemistry 264, no. 11 (April 1989): 6252–59. http://dx.doi.org/10.1016/s0021-9258(18)83341-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Nef, P., J. Heldman, D. Lazard, T. Margalit, M. Jaye, I. Hanukoglu, and D. Lancet. "Olfactory-specific Cytochrome P-450." Journal of Biological Chemistry 264, no. 12 (April 1989): 6780–85. http://dx.doi.org/10.1016/s0021-9258(18)83497-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Folkers, G. "Cytochrome P-450, 2nd ed." Pharmaceutica Acta Helvetiae 68, no. 4 (May 1994): 245. http://dx.doi.org/10.1016/0031-6865(94)90055-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Peter Guengerich, F. "Human cytochrome P-450 enzymes." Life Sciences 50, no. 20 (January 1992): 1471–78. http://dx.doi.org/10.1016/0024-3205(92)90136-d.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Court, Michael H. "Canine Cytochrome P-450 Pharmacogenetics." Veterinary Clinics of North America: Small Animal Practice 43, no. 5 (September 2013): 1027–38. http://dx.doi.org/10.1016/j.cvsm.2013.05.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Schenkman, John B., and Ingela Jansson. "Measurement of Cytochrome P-450." Current Protocols in Toxicology 00, no. 1 (May 1999): 4.1.1–4.1.14. http://dx.doi.org/10.1002/0471140856.tx0401s13.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Stiborová, Marie, and Hana Hansíková. "Cytochrome P-450 from Tulip Bulbs (Tulipa fosteriana L.) Oxidizes an Azo Dye Sudan I (1-Phenylazo-2-hydroxynaphthalene, Solvent Yellow 14) in vitro." Collection of Czechoslovak Chemical Communications 61, no. 11 (1996): 1689–96. http://dx.doi.org/10.1135/cccc19961689.

Full text

Abstract:

The microsomal fraction from tulip bulbs (Tulipa fosteriana L.) contains cytochrome P-450 enzymes catalyzing the NADPH-dependent oxidation of the xenobiotic substrate, an azo dye Sudan I (1-phenylazo-2-hydroxynaphthalene, Solvent Yellow 14). C-Hydroxy derivatives [1-(4-hydroxyphenylazo)-2-hydroxynaphthalene, 1-phenylazo-2,6-dihydroxynaphthalene, 1-(4-hydroxyphenylazo)-2,6-dihydroxynaphthalene] and the benzenediazonium ion are the products of the Sudan I oxidation. The oxidation of Sudan I has also been assessed in a reconstituted electron-transport chain with the isolated cytochrome P-450, isolated plant NADPH-cytochrome P-450 reductase and phospholipid. The results are discussed from the point of view of the role of cytochromes P-450 in the metabolism of xenobiotics in plants.

APA, Harvard, Vancouver, ISO, and other styles

32

Miles, J. S., A. W. Munro, B. N. Rospendowski, W. E. Smith, J. McKnight, and A. J. Thomson. "Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization." Biochemical Journal 288, no. 2 (December 1, 1992): 503–9. http://dx.doi.org/10.1042/bj2880503.

Full text

Abstract:

1. The gene CYP102 encoding cytochrome P-450 BM-3 and subgenes encoding the cytochrome P-450 and cytochrome P-450 reductase domains have been cloned in Escherichia coli. 2. The protein products of these genes have been overexpressed and purified to homogeneity. 3. The cytochrome P-450 domain is purified in the ferric low-spin state, but is readily converted into the high-spin state by addition of the substrate palmitate (Ks = 1 microM). The cytochrome P-450 reductase domain readily reduces cytochrome c. Mixing the two domains reconstitutes only about one-thousandth of the fatty acid hydroxylase activity associated with the intact cytochrome P-450 BM-3. 4. The X-band e.p.r. spectra of both the cytochrome P-450 domain and intact cytochrome P-450 BM-3 give g-values indicating low-spin ferric haem. The spectra are virtually identical with those of the equivalent form of cytochrome P-450 cam indicating that the haem ligation in cytochrome P-450 BM-3 is identical with that of cytochrome P-450 cam. 5. Resonance Raman spectra of the substrate-free and substrate-bound forms of the cytochrome P-450 domain are given. Spectral differences in comparison with cytochrome P-450 cam may reflect subtle electronic differences between the respective haem environments.

APA, Harvard, Vancouver, ISO, and other styles

33

Edwards, R. J., A. M. Singleton, B. P. Murray, D. Sesardic, K. J. Rich, D. S. Davies, and A. R. Boobis. "An anti-peptide antibody targeted to a specific region of rat cytochrome P-450IA2 inhibits enzyme activity." Biochemical Journal 266, no. 2 (March 1, 1990): 497–504. http://dx.doi.org/10.1042/bj2660497.

Full text

Abstract:

An anti-peptide antibody has been produced which binds to and specifically inhibits the activity of cytochrome P-450IA2 in rat hepatic microsomes. This was achieved by raising an antibody against a synthetic peptide (Ser-Glu-Asn-Tyr-Lys-Asp-Asn), the sequence of which occurs in cytochrome P-450IA2 at positions 290-296. The selection of this region of cytochrome P-450IA2 was based on several criteria, including prediction of surface and loop areas, identification of variable regions between cytochromes P-450IA2 and P-450IA1, and consideration of a site on cytochrome P-450IA1 where chemical modification has been shown to cause substantial enzyme inactivation. The specificity of antibody binding was determined by enzyme-linked immunosorbent assay and by immunoblotting using hepatic microsomal preparations and purified cytochrome P-450 isoenzymes. This showed that the antibody binds specifically to rat and mouse cytochrome P-450IA2 and to no other cytochrome P-450, as was predicted from the amino acid sequences of the peptide and the cytochromes P-450. The effect of the antibody upon enzyme activity was studied in hepatic microsomes from rats treated with 3-methylcholanthrene. The antibody was shown to inhibit specifically the activity of reactions catalysed by cytochrome P-450IA2 (phenacetin O-de-ethylase and 2-acetylaminofluorene activation), but had no effect on aryl hydrocarbon hydroxylase activity, which is catalysed by cytochrome P-450IA1, or on aflatoxin B1 activation.

APA, Harvard, Vancouver, ISO, and other styles

34

Stegeman, John J. "Cytochrome P-450 Cytochrome P-450: Structure, Mechanism, and Biochemistry Paul R. Ortiz de Montellano." BioScience 38, no. 6 (June 1988): 428–29. http://dx.doi.org/10.2307/1310936.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Coon, Minor J., and Dennis R. Koop. "Alcohol-inducible cytochrome P-450 (P-450ALC)." Archives of Toxicology 60, no. 1-3 (May 1987): 16–21. http://dx.doi.org/10.1007/bf00296940.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Barnes, T. S., P. M. Shaw, M. D. Burke, and W. T. Melvin. "Monoclonal antibodies against human cytochrome P-450 recognizing different pregnenolone 16α-carbonitrile-inducible rat cytochromes P-450." Biochemical Journal 248, no. 1 (November 15, 1987): 301–4. http://dx.doi.org/10.1042/bj2480301.

Full text

Abstract:

Six murine monoclonal antibodies against human hepatic cytochrome P-450 have been raised, using human liver microsomes (microsomal fractions) or semi-purified human cytochrome P-450 as immunogen. All six antibodies recognized the same highly purified of human liver cytochrome P-450 of molecular mass 53 kDa and gave rise to a single band at 53 kDa on immunoblots of human liver microsomes from 11 individuals. The antibodies also recognized proteins at 52 kDa and 54 kDa on immunoblots of control and induced male-rat liver microsomes, showing four different banding patterns. Antibodies HL4 and HP16 recognized a 52 kDa protein that was only weakly expressed in untreated rats and which was strongly induced by pregnenolone 16 alpha-carbonitrile (PCN) but not by phenobarbitone (PB), 3-methylcholanthrene (3MC), isosafrole (ISF), Aroclor 1254 (ARO), clofibrate or imidazole. HP10 and HL5 recognized a constitutive 52 kDa protein that was weakly induced by PCN but not by the other agents and was suppressed by 3MC and ARO. HP3 recognized a 54 kDa protein that was undetectable in control rats but was strongly induced by PB, PCN, ISF and ARO. HL3 appeared to recognize a combination of the proteins recognized by the other antibodies plus a 54 kDa protein that was weakly expressed in control rats. The constitutive proteins recognized were male-specific.

APA, Harvard, Vancouver, ISO, and other styles

37

Matuo, Míriam Cristina Sakuragui, Irene Satiko Kikuchi, and Terezinha de Jesus Andreoli Pinto. "Evaluation of cytochrome P-450 concentration in Saccharomyces cerevisiae strains." Brazilian Journal of Pharmaceutical Sciences 46, no. 3 (September 2010): 483–90. http://dx.doi.org/10.1590/s1984-82502010000300011.

Full text

Abstract:

Saccharomyces cerevisiae has been widely used in mutagenicity tests due to the presence of a cytochrome P-450 system, capable of metabolizing promutagens to active mutagens. There are a large number of S. cerevisiae strains with varying abilities to produce cytochrome P-450. However, strain selection and ideal cultivation conditions are not well defined. We compared cytochrome P-450 levels in four different S. cerevisiae strains and evaluated the cultivation conditions necessary to obtain the highest levels. The amount of cytochrome P-450 produced by each strain varied, as did the incubation time needed to reach the maximum level. The highest cytochrome P-450 concentrations were found in media containing fermentable sugars. The NCYC 240 strain produced the highest level of cytochrome P-450 when grown in the presence of 20 % (w/v) glucose. The addition of ethanol to the media also increased cytochrome P-450 synthesis in this strain. These results indicate cultivation conditions must be specific and well-established for the strain selected in order to assure high cytochrome P-450 levels and reliable mutagenicity results.

APA, Harvard, Vancouver, ISO, and other styles

38

Kühn-Velten, Nikolaus, Dagmar Bos, and Wolfgang Staib. "Differential down-regulation and induction responses of testicular steroidogenic cytochromes P-450(cscc) and P-450(C17α) to human choriogonadotropin." Bioscience Reports 6, no. 5 (May 1, 1986): 451–57. http://dx.doi.org/10.1007/bf01116136.

Full text

Abstract:

Evidence is presented that the regulation of the cytochrome P-450(C17α) of the steroid-17α-monooxygenase and of the cytochrome P-450(cscc) of the cholesterolmonooxygenase by human choriogonadotropin (hCG) in vivo is mediated by differential mechanisms in the adult rat testis. An initial down-regulation of the cytochrome P-450(C17α) but not of the P-450(cscc) can be demonstrated. Furthermore, induction of the cytochrome P-450(cscc) requires exposure to higher hCG doses (3270 of the maximal induction rate of 43.7 pmol/(testis x d) are achieved with 4 IU hCG/single dose) than induction of the P-450(C17α) (59% of the maximal induction rate of 48.4 pmol/(testis x d) with 4 IU hCG/single dose), Finally, induction ofcytochrome P-450(cscc) starts faster after initiation of hCG treatment than induction of P-450(C 17α).

APA, Harvard, Vancouver, ISO, and other styles

39

ITAKURA, Takao. "Superfamily of cytochrome P-450 genes." RADIOISOTOPES 40, no. 5 (1991): 204–11. http://dx.doi.org/10.3769/radioisotopes.40.5_204.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Guengerich, F. P., D. R. Umbenhauer, P. F. Churchill, P. H. Beaune, R. Böcker, R. G. Knodell, M. V. Martin, and R. S. Lloyd. "Polymorphism of human cytochrome P-450." Xenobiotica 17, no. 3 (January 1987): 311–16. http://dx.doi.org/10.3109/00498258709043941.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Ronis, M. J. J., and E. Hodgson. "Cytochrome P-450 monooxygenases in insects." Xenobiotica 19, no. 10 (January 1989): 1077–92. http://dx.doi.org/10.3109/00498258909043163.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Trager, William F. "Stereochemistry of Cytochrome P-450 Reactions." Drug Metabolism Reviews 20, no. 2-4 (January 1989): 489–96. http://dx.doi.org/10.3109/03602538909103555.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

BLACK, MARTIN. "Acetaminophen, Alcohol, and Cytochrome P-450." Annals of Internal Medicine 104, no. 3 (March 1, 1986): 427. http://dx.doi.org/10.7326/0003-4819-104-3-427.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

SHOUN, Hirofumi. "Fungal Denitrification and Cytochrome P-450." Journal of the agricultural chemical society of Japan 66, no. 2 (1992): 154–57. http://dx.doi.org/10.1271/nogeikagaku1924.66.154.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Koes, M. T., R. O. Stasiw, L. J. Forrester, S. K. Chattopadhyay, G. J. Bartung, D. Cowan, and H. D. Brown. "CHARACTERIZATION OF SOLUBILIZED CYTOCHROME P-450." International Journal of Peptide and Protein Research 5, no. 5 (January 12, 2009): 345–51. http://dx.doi.org/10.1111/j.1399-3011.1973.tb02338.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Guengerich, F. Peter, and Timothy L. Macdonald. "Mechanisms of cytochrome P‐450 catalysis." FASEB Journal 4, no. 8 (May 1990): 2453–59. http://dx.doi.org/10.1096/fasebj.4.8.2185971.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Cauwenbergh, Geert F. M. J., and Hugo F. A. Vanden Bossche. "Cytochrome P-450 and the Skin." International Journal of Dermatology 28, no. 8 (October 1989): 512. http://dx.doi.org/10.1111/j.1365-4362.1989.tb04601.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Loew, G. H., J. Collins, B. Luke, A. Waleh, and A. Pudzianowski. "Theoretical Studies of Cytochrome P-450." Enzyme 36, no. 1-2 (1986): 54–78. http://dx.doi.org/10.1159/000469278.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Hata, Masayuki, Yoshinori Hirano, Tyuji Hoshino, and Minoru Tsuda. "Monooxygenation Mechanism by Cytochrome P-450." Journal of the American Chemical Society 123, no. 26 (July 2001): 6410–16. http://dx.doi.org/10.1021/ja000908p.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Lewis, D. F. V. "Cytochrome P-450 and active oxygen." FEBS Letters 284, no. 1 (June 17, 1991): 134. http://dx.doi.org/10.1016/0014-5793(91)80782-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!