Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1986-11-17
pubmed:abstractText
A selection of inhibitors of rat and human neutrophil LTA4 hydrolases have been studied in vitro using partially purified enzymes. 5(S)trans 5,6 oxido-7,9-trans-11-cis-eicosatrienoic acid (LTA3) and 5(S)trans 5,6 oxido, 7,9-trans, 11,14,17-cis-eicosapentaenoic acid (LTA5) have been shown to inhibit neutrophil LTA4 hydrolases in a time-dependent manner. The products of hydrolysis of LTA3, LTA4 and LTA5 by human and rat neutrophil LTA4 hydrolase have been shown to displace [3H] LTB4 binding to human and rat neutrophil membranes. The order of displacement of [3H] LTB4 is LTB4 = LTB3 greater than LTB5 and this correlated well with their biological potencies for enhancement of neutrophil aggregation and chemokinesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0262-1746
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
167-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Neutrophil LTA4 hydrolases and leukotriene B4 receptors: effects of leukotriene epoxides and their enzymatic products.
pubmed:publicationType
Journal Article, Comparative Study