Linked Life Data

1713462

Source:http://linkedlifedata.com/resource/pubmed/id/1713462

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-8-29
pubmed:abstractText
Protein binding to both salicylate and 3H-labelled prostaglandin-E1 ([3H]PGE1) was examined in the sera of 22 allergic and 16 normal individuals. Protein binding to salicylate (P less than 0.001) and to [3H]PGE1 (P less than 0.01) was significantly greater in the allergic than in the normal group. The nature of the binding sites of salicylate and PGE1 was investigated with two fluorescent probes, dansylamide and dansylsarcosine as specific marker ligands for established Sites I and II, found to be specific for anionic drugs. The serum protein of 11 allergic subjects showed a higher binding at Site I (P less than 0.05) and a lower binding at Site II (P less than 0.05) than that of seven normal subjects. Salicylate and [3H]PGE1 bound competitively at the two sites. It was concluded, when comparing allergic to normal subjects, that the high protein binding of allergic individuals to salicylate and PGE1 could be attributed to qualitative and/or quantitative differences in the lipophilic substances which are tightly bound to the albumin of normal sera, causing a reduction in binding ability at Site I.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
609-15
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
High prostaglandin-E1 binding to serum protein in allergic subjects.
pubmed:affiliation
Department of Biochemistry for Health Science, School of Health Sciences, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
pubmed:publicationType
Journal Article