@prefix activity: .
@prefix address: .
@prefix agency: .
@prefix assay: .
@prefix assayCategory: .
@prefix assayTargetLink: .
@prefix biopax3: .
@prefix calbc: .
@prefix calbc-group: .
@prefix carrierLink: .
@prefix certainAgreement: .
@prefix chebi: .
@prefix chembl: .
@prefix chemicalCompound: .
@prefix chemicalCompoundRecord: .
@prefix clan: .
@prefix clinicalResult: .
@prefix clinicalStudy: .
@prefix clinicaltrials: .
@prefix company: .
@prefix confidenceScore: .
@prefix contact: .
@prefix country: .
@prefix cpath: .
@prefix curationLookup: .
@prefix dailymed: .
@prefix dailymed-drugs: .
@prefix dailymed-ingredient: .
@prefix dailymed-instance: .
@prefix databaseReference: .
@prefix dc: .
@prefix dc-term: .
@prefix diseaseontology: .
@prefix diseasome: .
@prefix diseasome-diseases: .
@prefix diseasome-gene: .
@prefix diseasome-instance: .
@prefix documentType: .
@prefix dosageForm: .
@prefix drug: .
@prefix drugbank: .
@prefix drugbank-proteinSequence: .
@prefix drugCategory: .
@prefix drugInteraction: .
@prefix drugTarget: .
@prefix eligibility: .
@prefix entrez-gene: .
@prefix entrez-goterm: .
@prefix entrezgene: .
@prefix enzymeLink: .
@prefix externalIdentifier: .
@prefix externalLink: .
@prefix factforge: .
@prefix family: .
@prefix foaf: .
@prefix formulation: .
@prefix freebase: .
@prefix gene-rif: .
@prefix geneontology: .
@prefix geneSequence: .
@prefix hapmap: .
@prefix indication: .
@prefix intervention: .
@prefix investigator: .
@prefix label: .
@prefix lhgdn: .
@prefix lifeskim: .
@prefix linkedct: .
@prefix linkedct-condition: .
@prefix linkedct-intervention: .
@prefix literatureCitation: .
@prefix lld: .
@prefix location: .
@prefix measurement: .
@prefix meddraSideEffect: .
@prefix mixture: .
@prefix molecularSpecies: .
@prefix molecule: .
@prefix moleculeType: .
@prefix ontotext: .
@prefix organismSpecies: .
@prefix outcomeAnalysis: .
@prefix outcomeMeasure: .
@prefix overallOfficial: .
@prefix owl: .
@prefix owlim: .
@prefix packager: .
@prefix participantFlow: .
@prefix patent: .
@prefix pfam: .
@prefix phenotype: .
@prefix pointOfContact: .
@prefix price: .
@prefix primaryOutcome: .
@prefix product: .
@prefix property: .
@prefix proteinSequence: .
@prefix pubmed: .
@prefix pubmed-article: .
@prefix pubmed-author: .
@prefix pubmed-mesh: .
@prefix pubmed-meshheading: .
@prefix pubmed-qualifier: .
@prefix rdf: .
@prefix rdfs: .
@prefix relationshipType: .
@prefix relontology: .
@prefix reportingGroup: .
@prefix researchStem: .
@prefix responsibleParty: .
@prefix result: .
@prefix resultsBaseline: .
@prefix resultsMeasure: .
@prefix resultsOutcome: .
@prefix secondaryOutcome: .
@prefix sideEffect: .
@prefix sideEffectFrequency: .
@prefix sider: .
@prefix sider-drug: .
@prefix skos: .
@prefix skos-xl: .
@prefix snp: .
@prefix structureType: .
@prefix studyMilestone: .
@prefix studyParticipants: .
@prefix studyPeriod: .
@prefix substructure: .
@prefix symptom: .
@prefix synonym: .
@prefix targetLink: .
@prefix targetType: .
@prefix taxonomy: .
@prefix taxonomyClass: .
@prefix taxonomyKingdom: .
@prefix transporterLink: .
@prefix umls: .
@prefix umls-concept: .
@prefix umls-label: .
@prefix umls-semnetwork: .
@prefix uniprot: .
@prefix uniprot-protein: .
@prefix uniprot-unstable: .
@prefix xsd: .
pubmed-article:9469594 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0205147 , umls-concept:C0450429 , umls-concept:C0070882 , umls-concept:C0085201 , umls-concept:C1455838 , umls-concept:C1514562 , umls-concept:C1883221 , umls-concept:C1167622 , umls-concept:C1883204 , umls-concept:C0205088 , umls-concept:C1880389 ;
pubmed:issue "1" ;
pubmed:dateCreated "1998-3-26" ;
pubmed:abstractText "The interaction of plasma phospholipid transfer protein (PLTP) with HDL has not been characterized in detail, although we have reported that the apoA-I/apoA-II molar ratio in the HDL particle influences PLTP-mediated HDL conversion, but not phospholipid transfer. The aim of this study was to examine whether PLTP binds apoA-I or apoA-II, and if this occurs, then determine the PLTP-binding domain of the apoA-I molecule. To study the PLTP/apolipoprotein interaction we used a solid phase ligand binding assay, the ELISA technique, and apoA-I and apoA-II affinity chromatography. PLTP bound to both apoA-I and apoA-II affinity columns, a finding subsequently utilized in the purification of PLTP. PLTP also bound to both apoA-I and apoA-II on ELISA plates in a concentration-dependent manner, and the binding could be displaced by preincubating the PLTP sample with purified apolipoproteins. To determine which portion of apoA-I is recognized by PLTP, we coated ELISA plates with either recombinant full-length apoA-I or three shortened apoA-I forms sequentially truncated from the C-terminus. To characterize the PLTP binding ability of the C-terminal region of apoA-I, we used both C-terminal CNBr-fragment and a synthetic C-terminal peptide of apoA-I. To further confirm the identity of the binding region, we probed the interaction with a polyclonal and several monoclonal anti-apoA-I antibodies. The antibodies that inhibited the interaction between PLTP and apoA-I were directed towards apoA-I epitopes localized between amino acids 27-141. The polyclonal antibody, R33, and the monoclonal antibody A-I-1 (epitope between amino acids 27-48) were most effective and reduced PLTP binding by 70%. These results show that PLTP binds to both apoA-I and apoA-II, and that the PLTP binding domain of apoA-I resides in the amino terminal region." ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , , , , , , , , ;
pubmed:status "MEDLINE" ;
pubmed:month "Jan" ;
pubmed:issn "0022-2275" ;
pubmed:author , pubmed-author:EhnholmCC , , pubmed-author:JauhiainenMM , pubmed-author:MetsoJJ , , ;
pubmed:issnType "Print" ;
pubmed:volume "39" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "152-61" ;
pubmed:dateRevised "2006-11-15" ;
pubmed:meshHeading pubmed-meshheading:9469594-Humans , pubmed-meshheading:9469594-Antibodies , , , , , , , , , , , , , ;
pubmed:year "1998" ;
pubmed:articleTitle "Binding of phospholipid transfer protein (PLTP) to apolipoproteins A-I and A-II: location of a PLTP binding domain in the amino terminal region of apoA-I." ;
pubmed:affiliation "National Public Health Institute, Department of Biochemistry, Helsinki, Finland." ;
pubmed:publicationType "Journal Article" , "Research Support, Non-U.S. Gov't" .