Linked Life Data

6125354

Source:http://linkedlifedata.com/resource/pubmed/id/6125354

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-10-12
pubmed:abstractText
Two hydrazines of clinical interest, the antidepressant drug phenelzine (PHZ) and the hepatotoxic metabolite of isoniazid, monoacetylhydrazine (MAH), were shown to be polymorphically acetylated by highly purified preparations of rabbit liver N-acetyltransferase (NAT). Both PHZ and MAH NAT activities exhibited purification and heat inactivation characteristics indistinguishable from genetically polymorphic NAT. Lineweaver-Burk analyses of PHZ and MAH NAT activities yielded apparent KM values of 4.18 mM for PHZ and 1.28 mM for MAH. These findings have implications concerning the structural requirements for polymorphic N-acetylation by liver NAT, and suggest that a wide variety of hydrazine compounds are also polymorphically N-acetylated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0090-9556
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
225-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
Polymorphic N-acetylation of phenelzine and monoacetylhydrazine by highly purified rabbit liver isoniazid N-acetyltransferase.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.