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dc.contributor.authorvan Loon, D.
dc.contributor.authorBerkhout, Theo
dc.contributor.authorDemel, R. A.
dc.contributor.authorWirtz, K. W. A.
dc.date.accessioned2014-06-11T09:00:34Z
dc.date.available2014-06-11T09:00:34Z
dc.date.issued1985-08-30
dc.identifier.citationvan Loon , D , Berkhout , T , Demel , R A & Wirtz , K W A 1985 , ' The lipid binding site of the phosphatidylcholine transfer protein from bovine liver ' , Chemistry and Physics of Lipids , vol. 38 , no. 1-2 , pp. 29-39 . https://doi.org/10.1016/0009-3084(85)90055-6
dc.identifier.issn0009-3084
dc.identifier.otherPURE: 7131031
dc.identifier.otherPURE UUID: f60caa62-7024-45ce-aa90-f54e3b4707dc
dc.identifier.otherPubMed: 4064223
dc.identifier.otherScopus: 0021969337
dc.identifier.urihttp://hdl.handle.net/2299/13690
dc.description.abstractThe phosphatidylcholine transfer protein (PC-TP) from bovine liver has a binding site for phosphatidylcholine (PC). Structural and molecular characteristics of this site were investigated by binding PC-analogues carrying photolabile, fluorescent and short-chain fatty acids. Analysis of the photolabeled PC/PC-TP adduct showed that the hydrophobic peptide segment Val171-Phe-Met-Tyr-Tyr-Phe-Asp177 is part of the lipid binding site for the 2-acyl chain. This site was further studied by binding PC carrying cis-parinaric acid at the sn-2-position. Time resolved fluorescence anisotropy measurements indicated that the 2-acyl chain was immobilized following the rotation of PC-TP. Similar experiments with PC carrying cis-parinaric acid at the sn-1-position demonstrated that the 1-acyl chain was immobilized as well but at a site distinctly different from that of the 2-acyl chain. Binding sites for the 1- and 2-acyl chain were then explored by use of PC-isomers carrying decanoic, lauric and myristic acid at the sn-1- (or sn-2-)-position and oleic acid at the sn-2- (or sn-1-)-position. Incubation with vesicles prepared of these PC-species indicated that binding to PC-TP diminished with decreasing acyl chain length but more so for species with short-chain fatty acids on the sn-2-position than on the sn-1-position. Transfer experiments confirmed that PC-TP discriminates between PC-isomers of apparently equal hydrophobicity favouring the transfer of these species carrying oleic acid at the sn-2-position.en
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofChemistry and Physics of Lipids
dc.subjectAndrogen-Binding Protein
dc.subjectAnimals
dc.subjectCarrier Proteins
dc.subjectCattle
dc.subjectFatty Acids
dc.subjectFluorescence Polarization
dc.subjectKinetics
dc.subjectLiver
dc.subjectModels, Biological
dc.subjectPeptide Fragments
dc.subjectPhosphatidylcholines
dc.subjectPhospholipid Transfer Proteins
dc.subjectProtein Binding
dc.subjectStructure-Activity Relationship
dc.titleThe lipid binding site of the phosphatidylcholine transfer protein from bovine liveren
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted1985-08-30
rioxxterms.versionofrecordhttps://doi.org/10.1016/0009-3084(85)90055-6
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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