File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Binding of bismuth to serum proteins: Implication for targets of Bi(III) in blood plasma

TitleBinding of bismuth to serum proteins: Implication for targets of Bi(III) in blood plasma
Authors
KeywordsAlbumin
Bismuth
Plasma
Toxicity
Transferrin
Issue Date2003
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal Of Inorganic Biochemistry, 2003, v. 94 n. 1-2, p. 114-120 How to Cite?
AbstractBismuth complexes have been widely used in clinical treatment as antiulcer drugs. However, different adverse effects have been observed and the diagnosis is generally confirmed by the detection of bismuth in blood or blood plasma. In this study, binding of bismuth to human serum albumin was studied by fluorescence spectroscopy with the binding constant log Ka to be 11.2. Competitive binding of bismuth to human albumin and transferrin was carried out at pH 7.4 by FPLC and ICP-MS. It was found that over 70% of bismuth binds to transferrin even in the presence of a large excess of albumin (albumin/transferrin = 13:1) at pH 7.4, 10 mM bicarbonate. The distribution of bismuth between the two proteins was almost unchanged when Cys34 of albumin was blocked. However, all bismuth binds to albumin when iron-saturated transferrin was used. Almost all of the bismuth was distributed over the fractions containing transferrin (70%) and albumin (<30%) in serum. The percentage of bismuth associated with transferrin was further increased by 15% with elevated transferrin in serum. Binding of bismuth to transferrin is much stronger than human albumin. Transferrin is probably the major target of bismuth in blood plasma, and it may play a role in the pharmacology of bismuth. © 2002 Elsevier Science Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/69431
ISSN
2023 Impact Factor: 3.8
2023 SCImago Journal Rankings: 0.614
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Hen_HK
dc.contributor.authorSzeto, KYen_HK
dc.date.accessioned2010-09-06T06:13:36Z-
dc.date.available2010-09-06T06:13:36Z-
dc.date.issued2003en_HK
dc.identifier.citationJournal Of Inorganic Biochemistry, 2003, v. 94 n. 1-2, p. 114-120en_HK
dc.identifier.issn0162-0134en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69431-
dc.description.abstractBismuth complexes have been widely used in clinical treatment as antiulcer drugs. However, different adverse effects have been observed and the diagnosis is generally confirmed by the detection of bismuth in blood or blood plasma. In this study, binding of bismuth to human serum albumin was studied by fluorescence spectroscopy with the binding constant log Ka to be 11.2. Competitive binding of bismuth to human albumin and transferrin was carried out at pH 7.4 by FPLC and ICP-MS. It was found that over 70% of bismuth binds to transferrin even in the presence of a large excess of albumin (albumin/transferrin = 13:1) at pH 7.4, 10 mM bicarbonate. The distribution of bismuth between the two proteins was almost unchanged when Cys34 of albumin was blocked. However, all bismuth binds to albumin when iron-saturated transferrin was used. Almost all of the bismuth was distributed over the fractions containing transferrin (70%) and albumin (<30%) in serum. The percentage of bismuth associated with transferrin was further increased by 15% with elevated transferrin in serum. Binding of bismuth to transferrin is much stronger than human albumin. Transferrin is probably the major target of bismuth in blood plasma, and it may play a role in the pharmacology of bismuth. © 2002 Elsevier Science Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbioen_HK
dc.relation.ispartofJournal of Inorganic Biochemistryen_HK
dc.rightsJournal of Inorganic Biochemistry. Copyright © Elsevier Inc.en_HK
dc.subjectAlbuminen_HK
dc.subjectBismuthen_HK
dc.subjectPlasmaen_HK
dc.subjectToxicityen_HK
dc.subjectTransferrinen_HK
dc.titleBinding of bismuth to serum proteins: Implication for targets of Bi(III) in blood plasmaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0162-0134&volume=94&spage=114&epage=120&date=2003&atitle=Binding+of+bismuth+to+serum+proteins:++implication+for+targets+of+Bi(III)+in+blood+plasmaen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0162-0134(02)00649-9en_HK
dc.identifier.pmid12620681-
dc.identifier.scopuseid_2-s2.0-0037293217en_HK
dc.identifier.hkuros76949en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037293217&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume94en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage114en_HK
dc.identifier.epage120en_HK
dc.identifier.isiWOS:000181499700015-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridSzeto, KY=7006866001en_HK
dc.identifier.issnl0162-0134-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats