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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-6-30
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pubmed:databankReference | |
pubmed:abstractText |
Humans possess two N-acetyltransferase isozymes (NAT1 and NAT2). We cloned and sequenced a novel NAT1 allele (Genbank HSU 80835) that contained nucleotide substitutions at -344 (C-->T), -40 (A-->T), 445 [G-->A(Val-->Ile)], 459 [G-->A(silent)], 640 [T-->G(Ser-->Ala)], a 9 base pair deletion between nucleotides 1065 and 1090, and 1095 (C-->A). The novel NAT1 allele which we have designated NAT1*17 is similar to NAT1*11 except for a G445A substitution (Val149-->Ile) in the NAT1 coding region. The G445A (Val149-->Ile) substitution yielded no significant changes in levels of immunoreactivity, as detected by Western blot, nor in intrinsic stability of the recombinant N-acetyltransferase protein. However, the G445A (Val149-->Ile) substitution yielded expression of recombinant NAT1 protein that catalyzed the N-acetylation of aromatic amines and the O- and N,O-acetylation of their N-hydroxylated metabolites at rates up to 2-fold higher than wild-type recombinant human NAT1.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arylamine N-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyltransferase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
233
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
584-91
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9168895-Acetylation,
pubmed-meshheading:9168895-Alleles,
pubmed-meshheading:9168895-Amino Acid Sequence,
pubmed-meshheading:9168895-Arylamine N-Acetyltransferase,
pubmed-meshheading:9168895-Base Sequence,
pubmed-meshheading:9168895-Binding Sites,
pubmed-meshheading:9168895-Chimera,
pubmed-meshheading:9168895-Cloning, Molecular,
pubmed-meshheading:9168895-DNA Primers,
pubmed-meshheading:9168895-Enzyme Stability,
pubmed-meshheading:9168895-Genetic Engineering,
pubmed-meshheading:9168895-Humans,
pubmed-meshheading:9168895-Isoenzymes,
pubmed-meshheading:9168895-Kinetics,
pubmed-meshheading:9168895-Male,
pubmed-meshheading:9168895-Polymerase Chain Reaction,
pubmed-meshheading:9168895-Polymorphism, Genetic,
pubmed-meshheading:9168895-Recombinant Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of a novel allele at the human NAT1 acetyltransferase locus.
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pubmed:affiliation |
Department of Pharmacology and Toxicology, University of North Dakota School of Medicine and Health Sciences, Grand Forks 58202-9037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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