Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1982-6-24
pubmed:abstractText
Chemical analysis of intact leukotriene A4 showed that vertebrate albumins prolonged its aqueous half-life. At pH 7.4, leukotriene A4 hydrolyzed by first order reaction kinetics with rate constants inversely proportional to the albumin concentration. The stabilizing effect of albumin varied quantitatively among different species. Certain agents, such as warfarin, that interact with the site I binding region of albumin reversed its stabilizing effect. Sequestration and exposure of leukotriene A4 to a hydrophobic, alkaline microenvironment of albumin would account for the results. The amino acid sequences Lys-Ala-Trp-Ala-Val-Ala-Arg from residues 211-217 of human albumin or Lys-Ala-Trp-Ser-Val-Ala-Arg from residues 210-216 of bovine albumin are compatible with this requirement. The persistence of leukotriene A4 in the presence of albumin confirms and extends our recent observations on its uniform and predictable influence on eicosanoid stability. The significance of this influence is uncertain; however, albumin can no longer be viewed as inert considering its capacity to modify the stability of several, structurally diverse eicosanoids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4680-3
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Albumin stabilizes leukotriene A4.
pubmed:publicationType
Journal Article