In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin
The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe2) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and μ, where...
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| Veröffentlicht in: | Biochemistry (Easton) 2010-12, Vol.49 (48), p.10261-10263 |
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| container_issue | 48 |
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| container_title | Biochemistry (Easton) |
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| creator | Ha-Duong, Nguyêt-Thanh Eid, Chantal Hémadi, Miryana El Hage Chahine, Jean-Michel |
| description | The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe2) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and μ, whereas the second does not. Dissociation constants were as follows: K 11Lf = 1.5 ± 0.2 μM, and K 12Lf = 11 ± 2 μM. Two slightly different interactions of T or TFe2 with Cp are detected for the first time. They are both independent of pH and μ and occur with 1:1 stoichiometry: K 1T = 19 ± 7 μM, and K 1TFe2 = 12 ± 4 μM. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis. |
| doi_str_mv | 10.1021/bi1014503 |
| format | Article |
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Cp interacts with two Lf molecules. The first interaction depends on pH and μ, whereas the second does not. Dissociation constants were as follows: K 11Lf = 1.5 ± 0.2 μM, and K 12Lf = 11 ± 2 μM. Two slightly different interactions of T or TFe2 with Cp are detected for the first time. They are both independent of pH and μ and occur with 1:1 stoichiometry: K 1T = 19 ± 7 μM, and K 1TFe2 = 12 ± 4 μM. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi1014503</identifier><identifier>PMID: 21049900</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Apoproteins - metabolism ; Ceruloplasmin - metabolism ; Humans ; Lactoferrin - metabolism ; Protein Binding ; Spectrometry, Fluorescence ; Thermodynamics ; Transferrin - metabolism</subject><ispartof>Biochemistry (Easton), 2010-12, Vol.49 (48), p.10261-10263</ispartof><rights>Copyright © 2010 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a380t-dcc288260894a0c1df1a7061973c91472b5a627ca47d02d55ad42930dd4f4e153</citedby><cites>FETCH-LOGICAL-a380t-dcc288260894a0c1df1a7061973c91472b5a627ca47d02d55ad42930dd4f4e153</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/bi1014503$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi1014503$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21049900$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ha-Duong, Nguyêt-Thanh</creatorcontrib><creatorcontrib>Eid, Chantal</creatorcontrib><creatorcontrib>Hémadi, Miryana</creatorcontrib><creatorcontrib>El Hage Chahine, Jean-Michel</creatorcontrib><title>In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe2) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and μ, whereas the second does not. Dissociation constants were as follows: K 11Lf = 1.5 ± 0.2 μM, and K 12Lf = 11 ± 2 μM. Two slightly different interactions of T or TFe2 with Cp are detected for the first time. They are both independent of pH and μ and occur with 1:1 stoichiometry: K 1T = 19 ± 7 μM, and K 1TFe2 = 12 ± 4 μM. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis.</description><subject>Apoproteins - metabolism</subject><subject>Ceruloplasmin - metabolism</subject><subject>Humans</subject><subject>Lactoferrin - metabolism</subject><subject>Protein Binding</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><subject>Transferrin - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0EFLwzAUB_AgipvTg19AchHxUH1Jk7Y5ynBuMPDg9FpekxQ62mQmLeK3t2O6k6fHe_z4w_sTcs3ggQFnj1XDgAkJ6QmZMskhEUrJUzIFgCzhKoMJuYhxO64CcnFOJpzBSACmZLFy9KPpg6cr19uAum-8o5Xtv6x1dG7D0Ppdi7FrHEVn6HLo0NG38d7RTUAXaxtC4y7JWY1ttFe_c0beF8-b-TJZv76s5k_rBNMC-sRozYuCZ1AogaCZqRnmkDGVp1oxkfNKYsZzjSI3wI2UaARXKRgjamGZTGfk7pC7C_5zsLEvuyZq27borB9iWXAmVZHle3l_kDr4GIOty11oOgzfJYNy31p5bG20N7-pQ9VZc5R_NY3g9gBQx3Lrh-DGJ_8J-gHdh3GE</recordid><startdate>20101207</startdate><enddate>20101207</enddate><creator>Ha-Duong, Nguyêt-Thanh</creator><creator>Eid, Chantal</creator><creator>Hémadi, Miryana</creator><creator>El Hage Chahine, Jean-Michel</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20101207</creationdate><title>In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin</title><author>Ha-Duong, Nguyêt-Thanh ; Eid, Chantal ; Hémadi, Miryana ; El Hage Chahine, Jean-Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a380t-dcc288260894a0c1df1a7061973c91472b5a627ca47d02d55ad42930dd4f4e153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Apoproteins - metabolism</topic><topic>Ceruloplasmin - metabolism</topic><topic>Humans</topic><topic>Lactoferrin - metabolism</topic><topic>Protein Binding</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><topic>Transferrin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ha-Duong, Nguyêt-Thanh</creatorcontrib><creatorcontrib>Eid, Chantal</creatorcontrib><creatorcontrib>Hémadi, Miryana</creatorcontrib><creatorcontrib>El Hage Chahine, Jean-Michel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ha-Duong, Nguyêt-Thanh</au><au>Eid, Chantal</au><au>Hémadi, Miryana</au><au>El Hage Chahine, Jean-Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2010-12-07</date><risdate>2010</risdate><volume>49</volume><issue>48</issue><spage>10261</spage><epage>10263</epage><pages>10261-10263</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe2) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and μ, whereas the second does not. Dissociation constants were as follows: K 11Lf = 1.5 ± 0.2 μM, and K 12Lf = 11 ± 2 μM. Two slightly different interactions of T or TFe2 with Cp are detected for the first time. They are both independent of pH and μ and occur with 1:1 stoichiometry: K 1T = 19 ± 7 μM, and K 1TFe2 = 12 ± 4 μM. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>21049900</pmid><doi>10.1021/bi1014503</doi><tpages>3</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Apoproteins - metabolism Ceruloplasmin - metabolism Humans Lactoferrin - metabolism Protein Binding Spectrometry, Fluorescence Thermodynamics Transferrin - metabolism |
| title | In Vitro Interaction between Ceruloplasmin and Human Serum Transferrin |
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