Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-2-25
pubmed:abstractText
New Zealand White rabbits were classified as rapid or slow acetylators by measuring the N-acetylation half-life of i.v. administered sulfadiazine, by pedigree analysis and by determination of liver N-acetyltransferase (NAT) activity in vitro. Slow acetylator rabbits were found to have significantly lower levels of p-aminobenzoic acid NAT activity in vitro than did rapid acetylator rabbits, demonstrating genetic covariation of p-aminobenzoic acid (monomorphic) and isoniazid (polymorphic) NAT activity. Monomorphic and polymorphic NAT activities could not be separated by two extensive purification procedures involving sequential centrifugation, fractional precipitation with ammonium sulfate, ion-exchange chromatography on DEAE-cellulose, gel filtration on Sephadex or Sephacryl and isoelectric focusing or electrophoresis on polyacrylamide gels. In addition, indistinguishable heat inactivation patterns were demonstrated for the two NAT activities utilizing highly purified NAT preparations at two different temperatures. Each of these findings support the coexistence of monomorphic and polymorphic NAT activities on a common protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Biochemical evidence for the coexistence of monomorphic and polymorphic N-acetyltransferase activities on a common protein in rabbit liver.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.