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http://purl.uniprot.org/citations/10329423http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10329423http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10329423http://www.w3.org/2000/01/rdf-schema#comment"The first step in the reaction of lecithin cholesterol acyltransferase (LCAT) with lipoproteins is the interfacial binding of the enzyme to the lipid surfaces. In this study the equilibrium dissociation constants (Kds) for the interaction of pure human plasma LCAT with LDL, HDL2, HDL3, and a reconstituted discoidal HDL (rHDL) were determined by the activity-inhibition method. In addition, enzyme kinetics were measured with each of the lipoprotein substrates. Based on phospholipid concentrations, the Kd values (0.9 x 10(-5) to 4.6 x 10(-5) M) increased in the order rHDL = HDL3 xsd:string
http://purl.uniprot.org/citations/10329423http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1999.0690"xsd:string
http://purl.uniprot.org/citations/10329423http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1999.0690"xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Durbin D."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Durbin D."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Jonas A."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Jonas A."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Kosek A.B."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/author"Kosek A.B."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/pages"548-551"xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/pages"548-551"xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/title"Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/title"Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins."xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/volume"258"xsd:string
http://purl.uniprot.org/citations/10329423http://purl.uniprot.org/core/volume"258"xsd:string
http://purl.uniprot.org/citations/10329423http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10329423
http://purl.uniprot.org/citations/10329423http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10329423
http://purl.uniprot.org/citations/10329423http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10329423
http://purl.uniprot.org/citations/10329423http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10329423