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Interference of UDP-glucuronyltransferase and beta-glucuronidase activity in rat liver microsomes at pH 7.5 with p-nitrophenol and p-nitrophenylglucuronide as substrates.
TLDR
Microsomal fraction contains the whole of hepatic UDP-glucuronyltransferase as well as part of beta-glUCuronidase, and was assayed under identical conditions using untreated male rat liver microsomes at pH 7.5.
Studies on the rate of reduction of hepatic microsomal cytochrome P-450 by reduced nicotinamide adenine dinucleotide phosphate: effect of drug substrates.
TLDR
The data suggest that the complexes formed between cytochrome P-450 and type I compounds are more readily reduced by NADPH than is the endogenous hemoprotein.
The distribution of the components of mixed-function oxidase between the rough and the smooth endoplasmic reticulum of liver cells.
TLDR
The results suggest that, in the rabbit, the rate-limiting step is the reduction of cytochrome P-450, and in the rat the difference in activities can be explained by differences in the concentration of cy tochromeP-450.
Changes in Michaelis and spectral constants for aniline in hepatic microsomes from phenobarbital-treated rats.
TLDR
It was found that the Michaelis constant and binding constant for aniline differ by a factor of 10 in microsomal preparations from intact animals, and phenobarbital treatment was found to elicit significant increases in both K[unknown] , and Km forAniline, implying that induction by phenobarBital may be associated with qualitative as well as quantitative changes in the hepaticmicrosomal anilines hydroxylase.
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