Academic literature on the topic 'Methylcholanthrene'

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Journal articles on the topic "Methylcholanthrene"

1

Arnold, P. S., R. C. Garner, and B. Tierney. "Purification and photoaffinity labelling of a rat cytosolic binding protein specific for 3-methylcholanthrene." Biochemical Journal 242, no. 2 (1987): 375–81. http://dx.doi.org/10.1042/bj2420375.

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Rat hepatic cytosolic proteins which sediment at 4-5 S on sucrose gradients exhibit high-affinity saturable binding for the carcinogen 3-methylcholanthrene. A rat liver protein of Stokes' radius 3 nm, Mr by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of 39,000 and with specific 3-methylcholanthrene-binding activity sedimenting at 4.5 S, has been purified 315-fold to apparent homogeneity by using affinity chromatography on a column of 1-hydroxy-3-methylcholanthrene coupled to epoxy-activated Sepharose 6B, in conjunction with two gel-filtration steps. The protein purified by this
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2

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 (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
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3

Lambrecht, R. W., J. M. Jacobs, P. R. Sinclair, and J. F. Sinclair. "Inhibition of uroporphyrinogen decarboxylase activity. The role of cytochrome P-450-mediated uroporphyrinogen oxidation." Biochemical Journal 269, no. 2 (1990): 437–41. http://dx.doi.org/10.1042/bj2690437.

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It was previously shown that uroporphyrinogen oxidation is catalysed by a form of cytochrome P-450 induced by 3-methylcholanthrene [Sinclair, Lambrecht & Sinclair (1987) Biochem. Biophys. Res. Commun. 146, 1324-1329]. We have now measured uroporphyrinogen oxidation and uroporphyrinogen decarboxylation simultaneously in 10,000 g supernatants from the livers of methylcholanthrene-treated mice and chick embryos incubated with an NADPH-generating system. We found that uroporphyrinogen oxidation is associated with inhibition of uroporphyrinogen decarboxylase activity. The decreased uroporphyrin
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4

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 (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 radioimmunoassa
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5

Seidel, S. L., and T. K. Shires. "Purification and characterization of a previously unreported form of cytochrome P-448 from the liver of 3-methylcholanthrene-pretreated rats." Biochemical Journal 235, no. 3 (1986): 859–68. http://dx.doi.org/10.1042/bj2350859.

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At least four hepatic isoenzymes of cytochrome P-450 were purified and characterized from rats treated with 3-methylcholanthrene. A monoclonal antibody developed against one of the forms (designated cytochrome P-450 MC-B) and polyclonal antibodies against others were used to demonstrate that form MC-B is immunologically distinct from other methylcholanthrene-inducible forms. Limited N-terminal amino acid sequencing showed that cytochrome P-450 MC-B has a primary structure that differs from the N-terminal sequences of other established rat isoenzymes. Cytochrome P-450 MC-B has a minimum Mr of 5
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6

Sinclair, P., J. Frezza, J. Sinclair, et al. "Immunochemical detection of different isoenzymes of cytochrome P-450 induced in chick hepatocyte cultures." Biochemical Journal 258, no. 1 (1989): 237–45. http://dx.doi.org/10.1042/bj2580237.

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This study investigated whether the same cytochrome P-450 (P-450) isoenzymes were inducible in cultures of chick-embryo hepatocytes as in the liver of chicken embryos. We purified two isoenzymes of cytochrome P-450 from the livers of 17-day-old-chick embryos: one of molecular mass approx. 50 kDa induced in vivo by the phenobarbital-like inducer glutethimide, and the second of approx. 57 kDa induced by 3-methylcholanthrene. Rabbit antiserum against the 50 kDa protein inhibited benzphetamine demethylase activity in hepatic microsomes (microsomal fractions) from glutethimide-treated chick embryo.
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7

Lutz, Charles T., Garvan Browne, and C. Rosemarie Petzold. "Methylcholanthrene causes increased thymocyte apoptosis." Toxicology 128, no. 2 (1998): 151–67. http://dx.doi.org/10.1016/s0300-483x(98)00043-2.

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8

Harvey, Ronald G., and Cecilia Cortez. "Synthesis of cholanthrene and 6-methylcholanthrene, biologically active analogs of the potent carcinogen 3-methylcholanthrene." Journal of Organic Chemistry 52, no. 2 (1987): 283–84. http://dx.doi.org/10.1021/jo00378a025.

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9

Laizé, Vincent, Paulo J. Gavaia, Marco Tarasco, et al. "Osteotoxicity of 3-methylcholanthrene in fish." Ecotoxicology and Environmental Safety 161 (October 2018): 721–28. http://dx.doi.org/10.1016/j.ecoenv.2018.06.035.

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10

Sheen, Yhun Y., Sun S. Kim, and Hea C. Yun. "Effect of 3-methylcholanthrene on rat uterus: Uterine growth and mechanism of action of 3-methylcholanthrene." Archives of Pharmacal Research 16, no. 4 (1993): 276–82. http://dx.doi.org/10.1007/bf02977516.

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