Linked Life Data

670218

Source:http://linkedlifedata.com/resource/pubmed/id/670218

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1978-9-30
pubmed:abstractText
Homogeneous preparations of the glutathione transferases from rat liver have been tested for their ability to catalyze a number of diverse nucleophilic reactions of GSH. Although disulfide interchange with GSSG or L-cystine, and cis-trans isomerization of maleic acid, are clearly promoted by thiols in solution, the reactions were not catalyzed by the glutathione transferases. In contrast, certain more hydrophobic analogs of these compounds were found to serve as substrates. The transferases also catalyze the glutathione-dependent release of p-nitrophenol from p-nitrophenyl acetate and p-nitrophenyl trimethylacetate. These observations are consistent with the formulation that catalysis may result from close juxtaposition of sufficiently electrophilic, nonpolar compounds with GSH on the enzyme surface.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5654-7
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Glutathione transferases. Catalysis of nucleophilic reactions of glutathione.
pubmed:publicationType
Journal Article