Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Patricia E. Levi"'
Autor:
Earl G. Alley, William H. Benson, William O. Berndt, Thomas W. Bouldin, Alan Brimfield, Leslee D. Brown, Lewis R. Brown, Jerry Browne, Philip Carl, Franklin R. Champlin, Howard Chambers, Janice E. Chambers, Lorris G. Cockerham, Robert K. Collins, Sue Conly-Danehower, Jon C. Cook, Nancy M. Cox, Kevin M. Crofton, Walter C. Dauterman, Walter J. Diehl, Donald N. Downer, Laurence Fishbein, Joyce E. Goldstein, Frank E. Guthrie, Doyle Graham, Raymond E. Grissom, John E. Harkness, Ernest Hodgson, Mary E. Hodgson, Clinton D. Kilts, Renate D. Kimbrough, Steven Kinsler, John S. Kizer, Cindy P. Lawler, Ross B. Leidy, Ann T. Lemley, Patricia E. Levi, Margaret Lewandowski, Mark H. Lewis, Kim E. Light, Morris A. Lipton, Richard B. Mailman, Beth Mileson, Pierre Morell, Toshio Narahashi, David E. Nichols, Deborah L. Novicki, Jerome J. Perry, Mario Perez-Reyes, Gary Peterson, Stephen B. Pruett, T. Wayne Schultz, Tony M. Shih, Ivin S. Silver, Gary Smith, Ronald E. Tynes, Mary Vore, Charles A. Waggoner, Quentin D. Walker, William Wargin, Charles L. Wax, John H. Weisburger, Christopher F. Wilkinson, Gary M. Williams, Dwayne A. Wise, John F. Young
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::709b8e81cfdacfdc90944b9024083d13
https://doi.org/10.1016/b978-0-12-420169-9.00033-3
https://doi.org/10.1016/b978-0-12-420169-9.00033-3
Publikováno v:
Pesticide Biochemistry and Physiology. 70:127-141
Several environmental chemicals are disruptive to the reproductive and endocrine systems of many species, including humans. Mechanisms for endocrine disruption are presently under scrutiny. Xenobiotic inducible mammalian cytochrome P450 (CYP) enzymes
Autor:
Randy L. Rose, Ernest Hodgson, Nathan J. Cherrington, Richard M. Philpot, Kieran M. Clements, Patricia E. Levi, J. Greg Falls
Publikováno v:
Journal of Biochemical and Molecular Toxicology. 12:205-212
Full-length cDNA clones encoding FMO1 and FMO5 have been isolated from a library constructed with mRNA from the liver of a female CD-1 mouse. The derived sequence of FMO1 contains 2310 bases: 1596 in the coding region, 301 in the 5'-flanking region,
Publikováno v:
Environmental Toxicology and Chemistry. 15:2293-2298
Livers from mallards (Anas platyrhynchos) were treated with either β-naphthoflavone (50 mg/kg) or phenobarbital (70 mg/kg). Purification of induced hepatic cytochrome P450 was accomplished using both DEAE and hydroxyapatite columns, as well as sodiu
Publikováno v:
Journal of Biochemical Toxicology. 10:171-177
Hepatic flavin-containing monooxygenase (FMO) activity of microsomes from adult CD-1, Swiss-Webster, C57BL/6, and DBA/2 mice was found to be significantly higher in females than in males. Based on protein and mRNA levels in CD-1 mice, FMO forms respo
Publikováno v:
Pesticide Biochemistry and Physiology. 46:15-26
The induction of the P450 isozymes 1a-1, 1a-2, and 2b-10 by four methylenedioxyphenyl (MDP) compounds, safrole (SAF), isosafrole (ISO), piperonyl butoxide (PBO), and sesamex (SES), and by the nonmethylenedioxyphenyl analog of SAF, allyl benzene (AB),
Publikováno v:
Chemico-Biological Interactions. 86:255-274
Regulation of cytochrome P-450 isozymes 1a-1, 1a-2, and 2b-10 by methylenedioxyphenyl compounds was studied by measuring levels of mRNA, protein, and enzyme activity in hepatic tissue from C57BL/6 (Ah+) and DBA/2 (Ah-) mice dosed with isosafrole (ISO
Publikováno v:
Pesticide Biochemistry and Physiology. 44:9-14
The herbicide synergist tridiphane [2-(3,5-dichlorophenyl)-2-(2,2,2,-trichloroethyl) oxirane] was examined for its ability to induced cytochrome P450 in vivo. Male C57BL/6N mice were given tridiphane, 250 mg/kg ip, for 3 days. Liver weight and P450 c
Autor:
Rama Misra, Ernest Hodgson, Alfred O. Inman, Nancy A. Monteiro-Riviere, Krishnappa Venkatesh, Patricia E. Levi
Publikováno v:
Pesticide Biochemistry and Physiology. 43:53-66
The cytochrome P450 (P450) content, the cytochrome c reductase activity, the metabolism of a variety of P450 substrates, and the presence and role of flavin-containing monooxygenase (FMO) in xenobiotic metabolism were studied in skin microsomes and c
Publikováno v:
Biochemical Pharmacology. 42:1411-1420
Flavin-containing monooxygenase (FMO; EC 1.14.13.8) was purified from mouse kidney microsomes and compared to that isolated from mouse liver microsomes. The purified enzymes from kidney and liver appeared as a single band on sodium dodecyi sulfate-po