Linked Life Data

3825174

Source:http://linkedlifedata.com/resource/pubmed/id/3825174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-4-10
pubmed:abstractText
The role of human foetal liver glutathione S-transferases in the detoxification of methyl parathion was investigated. Glutathione S-transferases were partially purified by affinity chromatography utilizing reduced glutathione as the ligand coupled to epoxy-activated Sepharose 4B. This resulted in the isolation of material with an average activity (mean +/- S.E.) of 58.90 +/- 4.83 mumol 1-chloro-2,4-dinitrobenzene conjugate formed/min per mg, representing a purification of 70-fold. These partially purified foetal liver transferases catalysed the metabolism of methyl parathion exclusively to desmethyl parathion via O-dealkylation. High-performance liquid chromatography, radiometric analysis of the enzymic reaction, and co-chromatography with reference standard on thin-layer chromatography confirmed the sole metabolite as desmethyl parathion. The range of foetal liver activity towards methyl parathion was from 30 to 122 nmol desmethyl parathion formed/min per mg. Analysis of the kinetic parameters of three partially purified foetal liver preparations with gestational ages of 14, 16 and 21 weeks resulted in Km values for methyl parathion of 0.24, 0.38 and 0.86 mM, respectively; whereas, the Km values assessed for glutathione were 0.20, 0.10 and 0.18 mM. The ability of human foetal liver glutathione S-transferases to catalyse the metabolism of methyl parathion exclusively to desmethyl parathion via O-dealkylation represents a major qualitative biochemical difference from the rat-liver isozymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0049-8254
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Biotransformation of methyl parathion by human foetal liver glutathione S-transferases: an in vitro study.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't