Results 181 to 190 of about 1,906,831 (271)

Liver microsomes and S9 from rainbow trout (Oncorhynchus mykiss): Comparison of basal-level enzyme activities with rat and determination of xenobiotic intrinsic clearance in support of bioaccumulation assessment

Environmental Toxicology and Chemistry, 2009
Xing Han, Diane L. Nabb, Ching-Hui Yang, S. Snajdr, R. Mingoia   +4 more
exaly   +2 more sources

The effects of gender, age, ethnicity, and liver cirrhosis on cytochrome P450 enzyme activity in human liver microsomes and inducibility in cultured human hepatocytes

Toxicology and Applied Pharmacology, 2004
A Parkinson, Andrew Parkinson
exaly   +2 more sources

Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians.

Journal of Pharmacology and Experimental Therapeutics, 1994
Interindividual variations in the level and activity of cytochrome P-450 enzymes were investigated in the liver microsomes of 30 Japanese and 30 Caucasian patients.
T. Shimada, H. Yamazaki, M. Mimura, Y. Inui, F. Guengerich   +4 more
semanticscholar   +1 more source

Metabolism of nitrosoacetoxymethylmethylamine in liver microsomes

Biochemical Pharmacology, 1981
Abstract The carcinogen nitrosoacetoxymethylmethylamine (NAMM)‡ was incubated with mouse liver microsomes. The decomposition rate of NAMM and the formation of methanol were determined. After addition of an NADPH-regenerating system, formaldehyde formation resulting from metabolic degradation of the methyl group of NAMM was measured.
K E, Appel, N, Frank, M, Wiessler
openaire   +2 more sources

Interaction of ranitidine with liver microsomes

Xenobiotica, 1982
1. Ranitidine interacts with liver microsomes from rats pretreated with different inducers of cytochrome P-450 to produce substrate difference optical spectra with a peak at 426-429 nm and a trough at 390-400 nm. 2. Cytochrome P-450 reduced with dithionite in the presence of ranitidine produced substrate difference spectra with a peak at 447 nm. 3.
S, Rendić, T, Alebić-Kolbah, F, Kajfez, H H, Ruf   +3 more
openaire   +2 more sources

Interaction of Cimetidine with Liver Microsomes

Xenobiotica, 1979
1. Ranitidine interacts with liver microsomes from rats pretreated with different inducers of cytochrome P-450 to produce substrate difference optical spectra with a peak at 426-429 nm and a trough at 390-400 nm. 2. Cytochrome P-450 reduced with dithionite in the presence of ranitidine produced substrate difference spectra with a peak at 447 nm. 3.
S, Rendić, V, Sunjić, R, Toso, F, Kajfez, H H, Ruf   +4 more
openaire   +2 more sources

Cytochrome P450 inhibitors. Evaluation of specificities in the in vitrometabolism of therapeutic agents by human liver microsomes.

Drug Metabolism And Disposition, 1995
Identifying selective inhibitors of cytochrome P450 isoforms is a useful tool in defining the role of individual cytochrome P450s in the metabolism process.
D. Newton, R. Wang, A. Y. Lu
semanticscholar   +1 more source

Permeability of Liver Microsomal Membranes to Glucose

Biochemical and Biophysical Research Communications, 1996
The permeability of rat liver microsomes to glucose has been studied by using (14)C-labelled D-glucose and a light-scattering technique. 1) The microsomal intravesicular apparent isotope space for D-glucose (1mM; after 5 min incubation at 22 degrees C) was 2.34 microl/mg protein, i.e., approximately 72% of the apparent water space.
MARCOLONGO, P., FULCERI, R., GIUNTI, R., BURCHELL, A., BENEDETTI, A.   +4 more
openaire   +4 more sources

A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes.

Journal of Pharmacology and Experimental Therapeutics, 1997
Nicotine is primarily metabolized to cotinine by cytochromes P450 (CYPs). The degree of variation in the metabolism of nicotine to cotinine and the relative roles of the polymorphic enzymes CYP2A6 and CYP2D6 in this metabolism were investigated.
E. Messina, R. Tyndale, E. Sellers
semanticscholar   +1 more source

Activation of Thionophosphates by Liver Microsomes

Nature, 1959
MANY organophosphorus insecticides are poor inhibitors of cholinesterase, but are converted to potent inhibitors (‘activated’) by certain mammalian and insect tissues. The activation by liver slices was first shown by Gardiner and Kilby1 for schradan (a phosphoroamidate), and by Diggle and Gage2 for parathion (a phosphorothionate). Davison3 showed that
openaire   +2 more sources