Linked Life Data

2721483

Source:http://linkedlifedata.com/resource/pubmed/id/2721483

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-7-10
pubmed:abstractText
The prevalent glyoxalase II (S-2-hydroxyacylglutathione hydrolase, EC 3.1.2.6, a form) of rat liver cytosol has been studied with a series of seven S-blocked glutathione derivatives. At pH 7.4 and 20 degrees C, only p-nitrobenzyl-S-glutathione was found completely inactive. All the other derivatives are linear competitive inhibitors of the enzyme. Ki values using S-D-lactoylglutathione as substrate are reported. Alkyl-S-glutathiones are weak inhibitors and their inhibition increases with the decrease of the length of the alkyl chain. The best inhibitors are those glutathione derivatives which contain a thioester bond (carbobenzoxy- and p-nitrocarbobenzoxy-S-glutathione) or a carbonyl group (p-chlorophenacyl-S-glutathione). Inhibition by carbobenzoxy-S-glutathione seems to be more complex since the double reciprocal plot shows deviation from linearity at low substrate concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0013-9432
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Effects of some S-blocked glutathione derivatives on the prevalent glyoxalase II (a form) of rat liver.
pubmed:affiliation
Department of Experimental Medicine, University of Perugia, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't