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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
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pubmed:dateCreated |
1989-7-12
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|
pubmed:abstractText |
Leukotriene C4 binding to mouse brain membranes was readily displaced by S-alkylglutathione derivatives, with the affinity of the test compound increasing as the alkyl chain length increases. S-decylglutathione was as potent as leukotriene C4. These data suggest that brain membrane leukotriene C4 binding sites are S-alkylglutathione binding sites, possibly microsomal glutathione transferase.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
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pubmed:month |
Feb
|
|
pubmed:issn |
0014-2999
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pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
161
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
99-101
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|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
|
pubmed:year |
1989
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|
pubmed:articleTitle |
Brain leukotriene C4 binding sites are S-alkylglutathione binding sites.
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|
pubmed:affiliation |
Positron Tomography Laboratory, University of Louvain, Louvain-la-Neuve, Belgium.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
