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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-2-25
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pubmed:abstractText |
Liver N-acetyltransferase (NAT) preparations (105,000 x g cytosol) were obtained from both sexes of 26 strains of inbred hamsters. Liver NAT activity levels were determined for six arylamine substrates; isoniazid, p-aminobenzoic acid (PABA), p-aminosalicylic acid (PAS), sulfamethazine (SMZ), procainamide and 2-aminofluorene. The N-acetylation of isoniazid, SMZ, procainamide and 2-aminofluorene exhibited a monomorphic expression in the hamster as the genetic variation in NAT activity levels between hamster strains was only about 2-fold for each substrate. In contrast, the N-acetylation of PABA and PAS showed a polymorphic expression in the hamster. Two inbred hamster lines (Bio 1.5 and Bio 82.73) had over 400-fold lower PABA NAT and over 20-fold lower PAS NAT activity levels than did the other inbred strains. In addition, the genetically determined N-acetylation differences between the rapid and slow acetylator hamster strains were also demonstrated in vivo for PABA but not for SMZ. Comparison of Michaelis-Menten kinetic constants of PABA NAT activity in a rapid and slow acetylator strain showed a 20-fold lower Km in the rapid acetylator strain suggesting an intrinsic structural difference in rapid and slow acetylator hamster liver NAT. Thus, the pharmacogenetic expression of the N-acetylation polymorphism is quite unique in the inbred hamster, in that PABA and PAS are genetically polymorphic substrates, whereas isoniazid, SMZ, procainamide and 2-aminofluorene are monomorphic, in direct contrast to man and rabbit.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-3565
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8-15
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7053425-Acetylation,
pubmed-meshheading:7053425-Acetyltransferases,
pubmed-meshheading:7053425-Animals,
pubmed-meshheading:7053425-Cricetinae,
pubmed-meshheading:7053425-Female,
pubmed-meshheading:7053425-Kinetics,
pubmed-meshheading:7053425-Male,
pubmed-meshheading:7053425-Mesocricetus,
pubmed-meshheading:7053425-Pharmaceutical Preparations,
pubmed-meshheading:7053425-Polymorphism, Genetic
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pubmed:year |
1982
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pubmed:articleTitle |
A unique pharmacogenetic expression of the N-acetylation polymorphism in the inbred hamster.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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