Linked Life Data

3040108

Source:http://linkedlifedata.com/resource/pubmed/id/3040108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-10-1
pubmed:abstractText
These studies investigated the effects of various serine proteinase inhibitors and substrates on the TCDD-binding capacity of the rat hepatic Ah receptor. TCDD binding to the Ah receptor was inhibited by serine proteinase inhibitors phenylmethylsulfonyl fluoride (PMSF), tosyl-lysine chloromethyl ketone (TosLysCH2Cl), tosylamide-phenylethyl chloromethyl ketone (TosPheCH2Cl) and substrates tosyl-L-arginine methyl ester (TosArgOMe) and D-tryptophan methyl ester (TrpOMe). The order of potency was TosPheCH2Cl greater than TosLysCH2Cl much greater than PMSF approximately equal to TosArgOMe approximately equal to TrpOMe. Reactivity of the chloromethyl ketones with sulfhydryl groups was suggested by their steep inhibition curves above the concentration of nonprotein sulfhydryl groups, and the partial mitigation of inhibition by 1 mM dithiothreitol. Inhibition by these reagents was irreversible, while that by TosArgOMe and TrpOMe was completely reversible by gel filtration. The mechanism of inhibition by TosArgOMe and TrpOMe was formally competitive, with inhibition constants similar to those reported in steroid hormone receptor systems. Neither inhibitors nor substrates displaced previously bound TCDD.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
925
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-16
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Influence of proteinase inhibitors and substrates on 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)-binding capacity of the rat hepatic Ah receptor.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.