Linked Life Data

3420615

Source:http://linkedlifedata.com/resource/pubmed/id/3420615

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-27
pubmed:abstractText
Glutathione S-transferase (GST) isoenzymes isolated from various human tissues are differentially inhibited by bile acids. Trihydroxy bile acid (lithocholate) was found to be more inhibitory to all the human GST isoenzymes tested in this study, as compared to the monohydroxy (cholate) and dihydroxy (chenodeoxycholate) bile acids. Among the three major classes of GST, mu class isoenzymes are generally inhibited to a greater extent than the alpha and pi class isoenzymes. The results of this study also indicate that differential inhibition of GST by various bile acids may be used to distinguish closely related GST isoenzymes within the mu class of GST isoenzyme. Likewise, the pi class or the anionic isoenzymes of human kidney, placenta, and erythrocytes can be distinguished using bile acid inhibition studies. These studies also provide further support for tissue-specific expression of GST isoenzymes in humans.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0041-008X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-54
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Inhibition of human glutathione S-transferases by bile acids.
pubmed:affiliation
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77550.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.