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Article: Competitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma
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TitleCompetitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma
 
AuthorsSun, H2 1
Li, H2
Mason, AB3
Woodworth, RC3
Sadler, PJ2
 
Issue Date2001
 
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
CitationJournal Of Biological Chemistry, 2001, v. 276 n. 12, p. 8829-8835 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M004779200
 
AbstractSeveral bismuth compounds are currently used as antiulcer drugs, but their mechanism of action is not well established. Proteins are thought to be target sites. In this work we establish that the competitive binding of Bi 3+ to the blood serum proteins albumin and transferrin, as isolated proteins and in blood plasma, can be monitored via observation of 1H and 13C NMR resonances of isotopically labeled [ε- 13C]Met transferrin. We show that Met132 in the I132M recombinant N-lobe transferrin mutant is a sensitive indicator of N-lobe metal binding. Bi3+ binds to the specific Fe3+ sites of transferrin and the observed shifts of Met resonances suggest that Bi 3+ induces similar conformational changes in the N-lobe of transferrin in aqueous solution and plasma. Bi3+ binding to albumin is nonspecific and Cys34 is not a major binding site, which is surprising because Bi3+ has a high affinity for thiolate sulfur. This illustrates that the potential target sites for metals (in this case Bi3+) in proteins depend not only on their presence but also on their accessibility. Bi3+ binds to transferrin in preference to albumin both in aqueous solution and in blood plasma.
 
ISSN0021-9258
2013 Impact Factor: 4.600
 
DOIhttp://dx.doi.org/10.1074/jbc.M004779200
 
ISI Accession Number IDWOS:000167607700031
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSun, H
 
dc.contributor.authorLi, H
 
dc.contributor.authorMason, AB
 
dc.contributor.authorWoodworth, RC
 
dc.contributor.authorSadler, PJ
 
dc.date.accessioned2010-09-06T06:08:45Z
 
dc.date.available2010-09-06T06:08:45Z
 
dc.date.issued2001
 
dc.description.abstractSeveral bismuth compounds are currently used as antiulcer drugs, but their mechanism of action is not well established. Proteins are thought to be target sites. In this work we establish that the competitive binding of Bi 3+ to the blood serum proteins albumin and transferrin, as isolated proteins and in blood plasma, can be monitored via observation of 1H and 13C NMR resonances of isotopically labeled [ε- 13C]Met transferrin. We show that Met132 in the I132M recombinant N-lobe transferrin mutant is a sensitive indicator of N-lobe metal binding. Bi3+ binds to the specific Fe3+ sites of transferrin and the observed shifts of Met resonances suggest that Bi 3+ induces similar conformational changes in the N-lobe of transferrin in aqueous solution and plasma. Bi3+ binding to albumin is nonspecific and Cys34 is not a major binding site, which is surprising because Bi3+ has a high affinity for thiolate sulfur. This illustrates that the potential target sites for metals (in this case Bi3+) in proteins depend not only on their presence but also on their accessibility. Bi3+ binds to transferrin in preference to albumin both in aqueous solution and in blood plasma.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationJournal Of Biological Chemistry, 2001, v. 276 n. 12, p. 8829-8835 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M004779200
 
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M004779200
 
dc.identifier.epage8835
 
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dc.identifier.isiWOS:000167607700031
 
dc.identifier.issn0021-9258
2013 Impact Factor: 4.600
 
dc.identifier.issue12
 
dc.identifier.openurl
 
dc.identifier.pmid11110794
 
dc.identifier.scopuseid_2-s2.0-0035937730
 
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dc.identifier.urihttp://hdl.handle.net/10722/68901
 
dc.identifier.volume276
 
dc.languageeng
 
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Biological Chemistry
 
dc.relation.referencesReferences in Scopus
 
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.
 
dc.titleCompetitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. University of Edinburgh
  3. University of Vermont