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Article: Competitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma

TitleCompetitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma
Authors
Issue Date2001
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2001, v. 276 n. 12, p. 8829-8835 How to Cite?
Abstract
Several 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.
Persistent Identifierhttp://hdl.handle.net/10722/68901
ISSN
2013 Impact Factor: 4.600
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong
  2. University of Edinburgh
  3. University of Vermont
DC FieldValueLanguage
dc.contributor.authorSun, Hen_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorMason, ABen_HK
dc.contributor.authorWoodworth, RCen_HK
dc.contributor.authorSadler, PJen_HK
dc.date.accessioned2010-09-06T06:08:45Z-
dc.date.available2010-09-06T06:08:45Z-
dc.date.issued2001en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2001, v. 276 n. 12, p. 8829-8835en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68901-
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.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.titleCompetitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasmaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=276&issue=12&spage=8829&epage=8835&date=2001&atitle=Competitive+binding+of+bismuth+to+transferrin+and+albumin+in+aqueous+solution+and+in+blood+plasmaen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M004779200en_HK
dc.identifier.pmid11110794en_HK
dc.identifier.scopuseid_2-s2.0-0035937730en_HK
dc.identifier.hkuros58752en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035937730&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume276en_HK
dc.identifier.issue12en_HK
dc.identifier.spage8829en_HK
dc.identifier.epage8835en_HK
dc.identifier.isiWOS:000167607700031-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridLi, H=14023043100en_HK
dc.identifier.scopusauthoridMason, AB=7203074416en_HK
dc.identifier.scopusauthoridWoodworth, RC=7006217057en_HK
dc.identifier.scopusauthoridSadler, PJ=7103024488en_HK

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