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http://purl.uniprot.org/citations/22264085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22264085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22264085http://www.w3.org/2000/01/rdf-schema#comment"Lupin seed globulin proteins form complexes with flavonoids, predominantly apigenin C-glycosides. Enzymes typical for the gastrointestinal tract were used to hydrolyze lupin seed globulins. Release of native flavonoids as a result of the proteolysis reaction was observed. Different analytical methods such as size exclusion chromatography, HPLC-MS, and fluorescence spectroscopy (steady-state fluorescence, fluorescence anisotropy, fluorescence lifetimes) were used for a detailed characterization of this phenomenon. Flavonoids liberated from lupin globulin proteins as a result of pancreatin-catalyzed digestion were bound by γ-conglutin resistant to this enzyme. Two possible mechanisms of this interaction may be suggested: hydrogen bonding between oligosaccharide chains of glycoproteins and the sugar moieties of the flavonoid glycosides or electrostatic attraction between positively charged γ-conglutin and flavonoids partially ionized at pH 7.5."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.org/dc/terms/identifier"doi:10.1021/jf2042592"xsd:string
http://purl.uniprot.org/citations/22264085http://purl.org/dc/terms/identifier"doi:10.1021/jf2042592"xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Czubinski J."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Czubinski J."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Dwiecki K."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Dwiecki K."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Kachlicki P."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Kachlicki P."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Lampart-Szczapa E."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Lampart-Szczapa E."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Neunert G."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Neunert G."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Nogala-Kalucka M."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Nogala-Kalucka M."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Siger A."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/author"Siger A."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/name"J. Agric. Food Chem."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/name"J. Agric. Food Chem."xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/pages"1830-1836"xsd:string
http://purl.uniprot.org/citations/22264085http://purl.uniprot.org/core/pages"1830-1836"xsd:string