Linked Life Data

8874825

Source:http://linkedlifedata.com/resource/pubmed/id/8874825

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-1-9
pubmed:abstractText
Nitroglycerin (GTN) has been used as the drug of choice in the treatment of angina pectoris. It has been shown that some glutathione S-transferases (GSTs) catalyze the metabolic conversion from GTN to glyceryl dinitrates (GDNs). In this study, we examined the substrate specificity of GSTs for GTN. Alpha and mu GSTs were isolated from porcine liver and intestinal mucosa by means of CM-cellulose and glutathione-affinity column chromatography. Mu GSTs degraded GTN time-dependently and formed 1,3-GDN in preference to 1,2-GDN as a ratio (1,2-GDN/ 1,3-GDN) of 0.61, whereas alpha GSTs formed twice as much 1,2-GDN as 1,3-GDN. These results showed that two GST families participate in the metabolic conversion of GTN at different hydrolyzing portions of the nitrogroups.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1093-6
pubmed:dateRevised
2007-10-3
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Variable glyceryl dinitrate formation as a function of glutathione S-transferase.
pubmed:affiliation
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't