Phenobarbital induction of cytochrome P-450 and UDP-glucuronosyltransferase in rabbit liver plasma membranes.
The presence of cytochrome P-450 and UDP-glucuronosyltransferase was confirmed in rabbit liver plasma membranes. Their levels, expressed as amount or activity/mg protein, were 25 and 40% respectively of those found in hepatic microsomes. Both enzymes were induced by phenobarbital treatment of the animals: administration of the barbiturate for 4 days, produced a 150% increase in the cytochrome P-450 content and in the specific activity of UDP-glucuronosyltransferase. As compared with the microsomal enzymes, the plasma membrane enzymes were localized in a lipid environment characterized by high levels of cholesterol and sphingomyelin and a low level of phosphatidylcholine. Treatment with phenobarbital for 4 days also caused a significant increase of phosphatidylcholine and phosphatidylethanolamine content in plasma membranes.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis*; D004790:Enzyme Induction; D014453:Glucuronosyltransferase / Q000096:biosynthesis*; D050356:Lipid Metabolism; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology*; D011817:Rabbits; D013347:Subcellular Fractions / Q000201:enzymology
D003577:Cytochrome P-450 Enzyme System; D014453:Glucuronosyltransferase; D010634:Phenobarbital