| pubmed-article:9250408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9250408 | lifeskim:mentions | umls-concept:C0023823 | lld:lifeskim |
| pubmed-article:9250408 | lifeskim:mentions | umls-concept:C0596040 | lld:lifeskim |
| pubmed-article:9250408 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:9250408 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9250408 | pubmed:dateCreated | 1997-12-2 | lld:pubmed |
| pubmed-article:9250408 | pubmed:abstractText | Free-radical oxidation of human low-density lipoprotein (LDL) produces levuglandin (LG)-protein adducts that were detected with an enzyme-linked immunosorbent assay using LGE2-KLH antibodies which recognize LGE2-derived pyrroles. The level of immunoreactivity increases with time of oxidation and reaches a maximum by 8 h. The yield of pyrrole varies nonlinearly with the level of LG adduction to LDL. At low LG:LDL ratios, such as those detected in oxidized LDL, the reaction of primary amino groups with LGE2 produces mostly non-pyrrole adducts that are not immunoreactive. Concomitant phospholipolysis must occur if the generation of immunoreactive epitopes in LDL involves oxidation of arachidonyl phospholipids. Thus, since a protein adduct prepared from synthetic LGE2-2-lysophosphatidylcholine ester showed, at most, only 0.5% cross-reactivity with the LGE2-KLH antibodies, the epitopes detected in oxidized LDL are almost certainly not protein adducts of LG-phospholipid esters. As expected, hydrolysis of the carboxylic ester in the protein adduct of LGE2-2-lysophosphatidylcholine ester by treatment with phospholipase A2 produced a fully immunoreactive LGE2-protein adduct. | lld:pubmed |
| pubmed-article:9250408 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9250408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9250408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9250408 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9250408 | pubmed:issn | 0893-228X | lld:pubmed |
| pubmed-article:9250408 | pubmed:author | pubmed-author:SinghUU | lld:pubmed |
| pubmed-article:9250408 | pubmed:author | pubmed-author:HoffH FHF | lld:pubmed |
| pubmed-article:9250408 | pubmed:author | pubmed-author:SalomonR GRG | lld:pubmed |
| pubmed-article:9250408 | pubmed:author | pubmed-author:O'NeilJJ | lld:pubmed |
| pubmed-article:9250408 | pubmed:author | pubmed-author:Subbanagounde... | lld:pubmed |
| pubmed-article:9250408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9250408 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:9250408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9250408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9250408 | pubmed:pagination | 750-9 | lld:pubmed |
| pubmed-article:9250408 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:meshHeading | pubmed-meshheading:9250408-... | lld:pubmed |
| pubmed-article:9250408 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9250408 | pubmed:articleTitle | Oxidation of low-density lipoproteins produces levuglandin-protein adducts. | lld:pubmed |
| pubmed-article:9250408 | pubmed:affiliation | Department of Chemistry, Case Western Reserve University, Cleveland, Ohio 44106-7078, USA. rgs@po.cwru.edu | lld:pubmed |
| pubmed-article:9250408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9250408 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:9250408 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9250408 | lld:pubmed |
