rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
1992-7-8
|
pubmed:abstractText |
Phosphonate analogue 5 of the lipid A precursor 4 has been prepared from phosphonate 2 and nucleotide 3 with the help of lipid A synthase, isolated from the overproducing Escherichia coli mutant MC 1061 (delta 2512) or JB1104 (delta 2514). The biological properties of phosphonate 5 and phosphate 4 are quite similar to each other as compared in the limulus amoebocyte lysate assay, by the activation of the RAW264 murine macrophagelike cell line (determined by stimulation of ornithine decarboxylase), and by the pyrogenicity in rabbits. Hydrolytic removal of the 1-phosphate group of 4 is thus not a prerequisite for its biological activity.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0022-2623
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
29
|
pubmed:volume |
35
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2070-4
|
pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1597857-Animals,
pubmed-meshheading:1597857-Body Temperature,
pubmed-meshheading:1597857-Escherichia coli,
pubmed-meshheading:1597857-Hexosyltransferases,
pubmed-meshheading:1597857-Limulus Test,
pubmed-meshheading:1597857-Lipid A,
pubmed-meshheading:1597857-Macrophage Activation,
pubmed-meshheading:1597857-Macrophages,
pubmed-meshheading:1597857-Mice,
pubmed-meshheading:1597857-Molecular Structure,
pubmed-meshheading:1597857-N-Acetylglucosaminyltransferases,
pubmed-meshheading:1597857-Organophosphorus Compounds,
pubmed-meshheading:1597857-Ornithine Decarboxylase,
pubmed-meshheading:1597857-Protein Precursors,
pubmed-meshheading:1597857-Rabbits,
pubmed-meshheading:1597857-Tumor Cells, Cultured
|
pubmed:year |
1992
|
pubmed:articleTitle |
Enzymatic synthesis and comparative biological evaluation of a phosphonate analogue of the lipid A precursor.
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pubmed:affiliation |
Sandoz Forschungsinstitut, Vienna, Austria.
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pubmed:publicationType |
Journal Article
|