Structural Features and Reversible Association of Different Quaternary Structures of β-Lactoglobulin
Structural and functional features were studied on the native dimeric form of β-lactoglobulin at neutral pH and on the monomeric forms obtained either by raising the pH to 9.0 or by blocking the thiol group of Cys121 with iodoacetamide under bland dissociating conditions. The thiol blocked monomer d...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1998-06, Vol.46 (6), p.2159-2166 |
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| container_issue | 6 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Iametti, Stefania Scaglioni, Leonardo Mazzini, Stefania Vecchio, Giuseppe Bonomi, Francesco |
| description | Structural and functional features were studied on the native dimeric form of β-lactoglobulin at neutral pH and on the monomeric forms obtained either by raising the pH to 9.0 or by blocking the thiol group of Cys121 with iodoacetamide under bland dissociating conditions. The thiol blocked monomer did not reassociate to native-like dimers, it retained retinol-binding ability, and it was found to display many of the structural features of the monomer obtained at pH 9, but differed in several structural features from the native dimer. The supramolecular associative properties of the proteins were studied by measuring concentration dependence of the accessibility of the backbone exchangeable amide protons in 1H NMR H/D exchange experiments, of their ligand-binding properties, and of their intrinsic fluorescence features. Evidence of reversible association was found for all the proteins with a very similar concentration dependence, indicating that the weak forces involved in this association were different from those stabilizing the native dimer. Keywords: β-Lactoglobulin; sulfhydryl groups; association equilibrium; ligand-binding properties |
| doi_str_mv | 10.1021/jf980004b |
| format | Article |
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The thiol blocked monomer did not reassociate to native-like dimers, it retained retinol-binding ability, and it was found to display many of the structural features of the monomer obtained at pH 9, but differed in several structural features from the native dimer. The supramolecular associative properties of the proteins were studied by measuring concentration dependence of the accessibility of the backbone exchangeable amide protons in 1H NMR H/D exchange experiments, of their ligand-binding properties, and of their intrinsic fluorescence features. Evidence of reversible association was found for all the proteins with a very similar concentration dependence, indicating that the weak forces involved in this association were different from those stabilizing the native dimer. 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Ice creams ; MOLECULAR CONFORMATION ; RETINOL ; SPECTRAL ANALYSIS ; SPECTROMETRIE ; SPECTROMETRY ; STRUCTURE ACTIVITY RELATIONSHIPS ; STRUCTURE CHIMIQUE ; THIOL ; THIOLS ; TIOLES</subject><ispartof>Journal of agricultural and food chemistry, 1998-06, Vol.46 (6), p.2159-2166</ispartof><rights>Copyright © 1998 American Chemical Society</rights><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a346t-6e10735dc99a9a640c912a6219951b633e5b9f2d05130f25090d1c93bfc377633</citedby><cites>FETCH-LOGICAL-a346t-6e10735dc99a9a640c912a6219951b633e5b9f2d05130f25090d1c93bfc377633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf980004b$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf980004b$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2275589$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Iametti, Stefania</creatorcontrib><creatorcontrib>Scaglioni, Leonardo</creatorcontrib><creatorcontrib>Mazzini, Stefania</creatorcontrib><creatorcontrib>Vecchio, Giuseppe</creatorcontrib><creatorcontrib>Bonomi, Francesco</creatorcontrib><title>Structural Features and Reversible Association of Different Quaternary Structures of β-Lactoglobulin</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Structural and functional features were studied on the native dimeric form of β-lactoglobulin at neutral pH and on the monomeric forms obtained either by raising the pH to 9.0 or by blocking the thiol group of Cys121 with iodoacetamide under bland dissociating conditions. The thiol blocked monomer did not reassociate to native-like dimers, it retained retinol-binding ability, and it was found to display many of the structural features of the monomer obtained at pH 9, but differed in several structural features from the native dimer. The supramolecular associative properties of the proteins were studied by measuring concentration dependence of the accessibility of the backbone exchangeable amide protons in 1H NMR H/D exchange experiments, of their ligand-binding properties, and of their intrinsic fluorescence features. Evidence of reversible association was found for all the proteins with a very similar concentration dependence, indicating that the weak forces involved in this association were different from those stabilizing the native dimer. Keywords: β-Lactoglobulin; sulfhydryl groups; association equilibrium; ligand-binding properties</description><subject>BETA-LACTOGLOBULIN</subject><subject>BETA-LACTOGLOBULINA</subject><subject>BETA-LACTOGLOBULINE</subject><subject>BINDING</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL STRUCTURE</subject><subject>ESPECTROMETRIA</subject><subject>ESTRUCTURA QUIMICA</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>LIGAND</subject><subject>LIGANDOS</subject><subject>LIGANDS</subject><subject>Milk and cheese industries. Ice creams</subject><subject>MOLECULAR CONFORMATION</subject><subject>RETINOL</subject><subject>SPECTRAL ANALYSIS</subject><subject>SPECTROMETRIE</subject><subject>SPECTROMETRY</subject><subject>STRUCTURE ACTIVITY RELATIONSHIPS</subject><subject>STRUCTURE CHIMIQUE</subject><subject>THIOL</subject><subject>THIOLS</subject><subject>TIOLES</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNptkMtOwzAQRS0EEqWw4AOQsoAFi8DYrpN4WQEFRMWjjw0ba-LaVUpIKjtB8Ft8CN-EUaArVrZ0zlzNXEIOKZxRYPR8ZWUGAIN8i_SoYBALSrNt0oMA40wkdJfseb8KSiZS6BEzbVyrm9ZhGY0Mho_xEVaLaGLejPNFXppo6H2tC2yKuopqG10W1hpnqiZ6arExrkL3Ef3FhOmgfH3GY9RNvSzrvC2Lap_sWCy9Ofh9-2Q-uppd3MTjh-vbi-E4Rj5ImjgxFFIuFlpKlJgMQEvKMGFUSkHzhHMjcmnZAgTlYJkACQuqJc-t5mkaeJ-cdrna1d47Y9XaFa9hP0VB_fSjNv0E97hz1-g1ltZhpQu_GWAsFSKTQYs7rfCNed9gdC8qSXkq1Oxxqu5nE2B3ybNiwT_qfIu1wqULkfNpOCAFySkbBH7ScdRereo21Ff6f9b7Bokliec</recordid><startdate>19980601</startdate><enddate>19980601</enddate><creator>Iametti, Stefania</creator><creator>Scaglioni, Leonardo</creator><creator>Mazzini, Stefania</creator><creator>Vecchio, Giuseppe</creator><creator>Bonomi, Francesco</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19980601</creationdate><title>Structural Features and Reversible Association of Different Quaternary Structures of β-Lactoglobulin</title><author>Iametti, Stefania ; Scaglioni, Leonardo ; Mazzini, Stefania ; Vecchio, Giuseppe ; Bonomi, Francesco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a346t-6e10735dc99a9a640c912a6219951b633e5b9f2d05130f25090d1c93bfc377633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>BETA-LACTOGLOBULIN</topic><topic>BETA-LACTOGLOBULINA</topic><topic>BETA-LACTOGLOBULINE</topic><topic>BINDING</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL STRUCTURE</topic><topic>ESPECTROMETRIA</topic><topic>ESTRUCTURA QUIMICA</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>LIGAND</topic><topic>LIGANDOS</topic><topic>LIGANDS</topic><topic>Milk and cheese industries. Ice creams</topic><topic>MOLECULAR CONFORMATION</topic><topic>RETINOL</topic><topic>SPECTRAL ANALYSIS</topic><topic>SPECTROMETRIE</topic><topic>SPECTROMETRY</topic><topic>STRUCTURE ACTIVITY RELATIONSHIPS</topic><topic>STRUCTURE CHIMIQUE</topic><topic>THIOL</topic><topic>THIOLS</topic><topic>TIOLES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iametti, Stefania</creatorcontrib><creatorcontrib>Scaglioni, Leonardo</creatorcontrib><creatorcontrib>Mazzini, Stefania</creatorcontrib><creatorcontrib>Vecchio, Giuseppe</creatorcontrib><creatorcontrib>Bonomi, Francesco</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iametti, Stefania</au><au>Scaglioni, Leonardo</au><au>Mazzini, Stefania</au><au>Vecchio, Giuseppe</au><au>Bonomi, Francesco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Features and Reversible Association of Different Quaternary Structures of β-Lactoglobulin</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1998-06-01</date><risdate>1998</risdate><volume>46</volume><issue>6</issue><spage>2159</spage><epage>2166</epage><pages>2159-2166</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Structural and functional features were studied on the native dimeric form of β-lactoglobulin at neutral pH and on the monomeric forms obtained either by raising the pH to 9.0 or by blocking the thiol group of Cys121 with iodoacetamide under bland dissociating conditions. The thiol blocked monomer did not reassociate to native-like dimers, it retained retinol-binding ability, and it was found to display many of the structural features of the monomer obtained at pH 9, but differed in several structural features from the native dimer. The supramolecular associative properties of the proteins were studied by measuring concentration dependence of the accessibility of the backbone exchangeable amide protons in 1H NMR H/D exchange experiments, of their ligand-binding properties, and of their intrinsic fluorescence features. Evidence of reversible association was found for all the proteins with a very similar concentration dependence, indicating that the weak forces involved in this association were different from those stabilizing the native dimer. Keywords: β-Lactoglobulin; sulfhydryl groups; association equilibrium; ligand-binding properties</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf980004b</doi><tpages>8</tpages></addata></record> |
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| issn | 0021-8561 1520-5118 |
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| source | American Chemical Society (ACS) Journals |
| subjects | BETA-LACTOGLOBULIN BETA-LACTOGLOBULINA BETA-LACTOGLOBULINE BINDING Biological and medical sciences CHEMICAL STRUCTURE ESPECTROMETRIA ESTRUCTURA QUIMICA Food industries Fundamental and applied biological sciences. Psychology LIGAND LIGANDOS LIGANDS Milk and cheese industries. Ice creams MOLECULAR CONFORMATION RETINOL SPECTRAL ANALYSIS SPECTROMETRIE SPECTROMETRY STRUCTURE ACTIVITY RELATIONSHIPS STRUCTURE CHIMIQUE THIOL THIOLS TIOLES |
| title | Structural Features and Reversible Association of Different Quaternary Structures of β-Lactoglobulin |
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