Wendell W. Weber

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An inbred mouse model for the human N-acetylation polymorphism has been used to investigate the biochemical basis for the arylamine N-acetylation polymorphism and the relationship between the cytosolic enzymes arylamine N-acetyltransferase (NAT), arylhydroxamic acid N,O-acyltransferase, and N-hydroxyarylamine O-acetyltransferase. Biochemical studies of(More)
A consolidated classification system is described for prokaryotic and eukaryotic N-acetyltransferases in accordance with the international rules for gene nomenclature. The root symbol (NAT) specifically identifies the genes that code for the N-acetyltransferases, and NAT* loci encoding proteins with similar function are distinguished by Arabic numerals.(More)
This article is a report on a symposium sponsored by the American Society for Pharmacology and Experimental Therapeutics presented at the joint meeting of the American Society for Biochemistry and Molecular Biology and the American Society for Pharmacology and Experimental Therapeutics, June 4–8, Boston, Massachusetts. The presentations focused on the(More)
Two human acetyl-CoA:arylamine N-acetyltransferases (NAT1 and NAT2) have been identified. Therapeutic and carcinogenic agents that are substrates for these isoenzymes (including isoniazid, sulfamethazine, p-aminobenzoic acid, 5-aminosalicyclic acid, and 2-aminofluorene) have been used to evaluate the role of the N-acetylation polymorphisms of NAT1 and NAT2(More)
Kinetic parameters for arylamine N-acetyltransferase activity in liver, blood, and bladder from C57BL/6J and A/J mouse strains were determined using an improved assay system, and some deviations were found from previously reported results. In the present studies, blood N-acetyltransferase activity with p-aminobenzoic acid and 2-aminofluorene as substrates(More)
Investigations in the rabbit have indicated the existence of more than one N-acetyltransferase (EC At least two enzymes, possibly isoenzymes, were partially characterized. The enzymes differed in their tissue distribution, substrate specificity, stability and pH characteristics. One of the enzymes was primarily associated with liver and gut and(More)
A survey among 20 inbred mouse strains revealed large variation (up to approximately 20-fold) for the N-acetylation of p-aminobenzoic acid by blood N-acetyltransferase and for the aromatic amine carcinogen benzidine by both liver and blood N-acetyltransferase. Of 20 strains surveyed, three are classified as slow acetylators (A/J, AHe/J, and X/Gf) and 17 are(More)
The distribution of N-acetyltransferase (NAT) activity in 35 tissues of inbred rapid acetylator C57BL/6J and slow acetylator congenic B6.A-NatS mice was determined by incubation of tissue cytosols with 2-aminofluorene or p-aminobenzoic acid followed by HPLC assay. Tissues examined included the gastrointestinal tract, lymphoid tissues, skin, blood(More)
N-Acetylation plays an important role in the metabolism of a wide variety of hydrazine drugs and arylamine drugs and carcinogens. Humans have genetically determined differences in their N-acetyltransferase activities and are phenotypically classified as rapid or slow acetylators. Mice have a similar genetic polymorphism in N-acetyltransferase activity and(More)