Abstract
Acetyl CoA-dependent arylamine N-acetyltransferase (EC 2.3.1.5) is the target of a genetic polymorphism in the metabolism of drugs and carcinogens. N-Acetyltransferase was purified 1000-fold from cytosol of human liver and its identity was verified by amino acid sequence homology of two of its tryptic peptides with published rabbit and chicken N-acetyltransferase sequences. Enzyme activity correlated with the presence of two proteins, NAT-1 and NAT-2, with indistinguishable molecular masses (31 kDa). NAT-1 and NAT-2 could be separated by anion-exchange chromatography and were functionally distinguished by their different apparent affinities for the acceptor amine sulfamethazine (SMZ). Antibodies raised against NAT-1 were able to recognize both isozymes on Western blots.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / isolation & purification*
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Amino Acid Sequence
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Animals
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Arylamine N-Acetyltransferase / genetics
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Arylamine N-Acetyltransferase / isolation & purification*
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Arylamine N-Acetyltransferase / metabolism
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Blotting, Western
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Chickens
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Humans
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Isoenzymes / genetics
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Isoenzymes / isolation & purification*
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Isoenzymes / metabolism
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Liver / enzymology*
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments
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Polymorphism, Genetic
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Rabbits
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Sequence Homology, Nucleic Acid
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Substrate Specificity
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Sulfamethazine / metabolism
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Trypsin
Substances
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Isoenzymes
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Peptide Fragments
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Sulfamethazine
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Acetyltransferases
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Arylamine N-Acetyltransferase
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Trypsin