Purification and characterization of cytochrome P450 isozymes from ß/beta-naphthoflavone-induced adult hen liver.
Gupta-RP; Lapadula-DM; Abou-Donia-MB
Arch Biochem Biophys 1990 Jan; 282(1):170-182
Cytochrome-P450 isozymes induced in hens by a classic polycyclic aromatic hydrocarbon beta-naphthoflavone (6051872) were isolated and characterized. Adult leghorn-hens were injected intraperitoneally with 2% beta-naphthoflavone at 80mg/kg daily for 4 days; 24 hours after the last dose, hens were killed, and the liver microsomes were isolated. The isolation procedure was a modification of the method used for purifying cytochrome-P450 isozymes from phenobarbital (PB) induced hen livers. Cytochromes-P450 beta-NF-A1/beta-NF-A2 were identical or very similar to PB induced PB-A, as all of them exhibited almost the same amino terminal sequence, mobilities during one and two dimensional electrophoresis, and other properties. The other two immunochemically related cytochrome-P450s, beta-NF-B and beta-NF-C, were distinct isozymes with different N-terminal amino acid sequences, and several biophysical and biochemical properties. The amino terminal sequences of cytochrome-P450 beta-NF-B and beta- NF-C were also different from other cytochrome-P450s purified from mammalian or nonmammalian species. The authors conclude that purification of these P450s and availability of antiserums will be useful in examining their role in the metabolism of various environmental neurotoxic compounds.
NIOSH-Publication; NIOSH-Grant; Neurotoxic-effects; Enzyme-activity; Nervous-system-disorders; Laboratory-animals; Liver-microsomal-enzymes; Chemical-structure
Pharmacology Duke University Department of Pharmacology Durham, N C 27710
Neurotoxic Disorders; Neurotoxic-effects
Archives of Biochemistry and Biophysics
Duke University, Durham, North Carolina