Results 211 to 220 of about 17,285 (228)
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Evidence for arylamine N-acetyltransferase in the nematode Anisakis simplex
Cancer Letters, 1996N-Acetyltransferase activities with p-aminobenzoic acid and 2-aminofluorene were determined in Anisakis simplex, a nematode found in the intestine of the salt water fish Trichiurus lepturus. The N-acetyltransferase activity was determined using an acetyl CoA recycling assay and high pressure liquid chromatography.
H. M. Kuo +7 more
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Arylamine N-acetyltransferase in human red blood cells
Biochemical Pharmacology, 1992N-Acetyltransferase activities associated with erythrocytes from 20 individuals have been determined with p-aminobenzoic acid as substrate. A three-fold variation in Vmax is found. The N-acetyltransferase genotype of the individuals has been determined and there is no correlation between the extent of acetylation measured in the individuals ...
Edith Sim +3 more
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Effect of Environmental Substances on the Activity of Arylamine N-Acetyltransferases
Current Drug Metabolism, 2008Arylamine N-acetyltransferases (NAT) are xenobiotic-metabolizing enzymes responsible for the acetylation of many aromatic arylamine and heterocyclic amines, thereby playing an important role in both detoxification and activation of numerous drugs and carcinogens. Two closely related isoforms (NAT1 and NAT2) have been described in humans. NAT2 is mainly
Julien Dairou +2 more
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Carcinogenesis, 1993
Carcinogenic arylamines are acetylated by the hepatic N-acetyltransferase. This enzyme is polymorphic in humans and in some epidemiological studies, the slow-acetylator phenotype has been associated with higher risk of bladder cancer and lower risk of ...
D. Bell +7 more
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Carcinogenic arylamines are acetylated by the hepatic N-acetyltransferase. This enzyme is polymorphic in humans and in some epidemiological studies, the slow-acetylator phenotype has been associated with higher risk of bladder cancer and lower risk of ...
D. Bell +7 more
semanticscholar +1 more source
Structure and Regulation of the Drug-Metabolizing Enzymes Arylamine N-acetyltransferases
Current Medicinal Chemistry, 2005Arylamine N-acetyltransferases (NAT) are xenobiotic-metabolizing enzymes responsible for N-acetylation of many arylamines. They are also important for O-acetylation of N-hydroxylated heterocyclic amines. These enzymes play thus an important role in the detoxification and activation of numerous therapeutic drugs and carcinogens.
Jean-Marie Dupret +1 more
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Arylamine N-acetyltransferase 1 (NAT1) genotypes in a Lebanese population
Pharmacogenetics, 2000The frequency distributions of human N-acetyltransferase 1 (NAT1*) alleles in various ethnic groups are largely unknown. This lack of information is in contrast to the many studies of ethnic differences in NAT2* alleles and phenotypes. Increasing interest in NAT1 due to its potential roles in carcinogen metabolism and cancer risk makes it desirable to ...
Hassan R. Dhaini, Gerald N. Levy
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Sheep Tissue Acetyl Coenzyme A-Dependent Arylamine N-Acetyltransferases
Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, 1997Acetyl coenzyme A-dependent arylamine N-acetyltransferases (NATs), EC 2.3.1.5. were measured in sheep tissues (N = 14) using p-aminobenzoic acid (PABA) as a substrate. Specific activities of liver, kidney, and lung NATs were 5.3 x 10(-3) +/- 1.4 (mean +/- SE) nmoles.min-1.mg protein-1, 3.4 x 10(-3) +/- 1.1 nmoles.min-1.mg protein-1, 2.5 x 10(-3) +/- 1 ...
Tugba Guvenc, Tülin Güray
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Pharmacogenomics of Arylamine N-acetyltransferase
Current Pharmacogenomics, 2004Valerie Cornish +2 more
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