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Article: N-lobe versus C-lobe complexation of bismuth by human transferrin

TitleN-lobe versus C-lobe complexation of bismuth by human transferrin
Authors
KeywordsMetal binding
NMR spectroscopy
Protein conformation
Serum protein
Stability constant
Issue Date1999
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1999, v. 337 n. 1, p. 105-111 How to Cite?
AbstractInteractions of recombinant N-lobe of human serum transferrin (hTF/2N) with Bi3+, a metal ion widely used in medicine, have been investigated by both UV and NMR spectroscopy. The bicarbonate-independent stability constant for Bi3+ binding (K*) to hTF/2N was determined to be log K* 18.9 ± 0.2 in 5 mM bicarbonate/10 mM Hepes buffer at 310 K, pH 7.4. The presence of Fe3+ in the C-lobe of intact hTF perturbed Bi3+ binding to the N-lobe, whereas binding of Bi3+ to the C-lobe was unaffected by the presence of Fe3+ in the N-lobe. Reactions of Bi3+ (as bismuth nitrilotriacetate or ranitidine bismuth citrate) with hTF/2N in solutions containing 10 mM bicarbonate induced specific changes to high-held 1H-NMR peaks. The 1H co-ordination shifts induced by Bi3+ were similar to those induced by Fe3+ and Ga3+, suggesting that Bi3+ binding causes similar structural changes to those induced by hTF/2N. 13C-NMR data showed that carbonate binds to hTF/2N concomitantly with Bi3+.
Persistent Identifierhttp://hdl.handle.net/10722/69628
ISSN
2014 Impact Factor: 4.396
2014 SCImago Journal Rankings: 2.424
PubMed Central ID
ISI Accession Number ID
References

 

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.accessioned2010-09-06T06:15:24Z-
dc.date.available2010-09-06T06:15:24Z-
dc.date.issued1999en_HK
dc.identifier.citationBiochemical Journal, 1999, v. 337 n. 1, p. 105-111en_HK
dc.identifier.issn0264-6021en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69628-
dc.description.abstractInteractions of recombinant N-lobe of human serum transferrin (hTF/2N) with Bi3+, a metal ion widely used in medicine, have been investigated by both UV and NMR spectroscopy. The bicarbonate-independent stability constant for Bi3+ binding (K*) to hTF/2N was determined to be log K* 18.9 ± 0.2 in 5 mM bicarbonate/10 mM Hepes buffer at 310 K, pH 7.4. The presence of Fe3+ in the C-lobe of intact hTF perturbed Bi3+ binding to the N-lobe, whereas binding of Bi3+ to the C-lobe was unaffected by the presence of Fe3+ in the N-lobe. Reactions of Bi3+ (as bismuth nitrilotriacetate or ranitidine bismuth citrate) with hTF/2N in solutions containing 10 mM bicarbonate induced specific changes to high-held 1H-NMR peaks. The 1H co-ordination shifts induced by Bi3+ were similar to those induced by Fe3+ and Ga3+, suggesting that Bi3+ binding causes similar structural changes to those induced by hTF/2N. 13C-NMR data showed that carbonate binds to hTF/2N concomitantly with Bi3+.en_HK
dc.languageengen_HK
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_HK
dc.relation.ispartofBiochemical Journalen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectMetal bindingen_HK
dc.subjectNMR spectroscopyen_HK
dc.subjectProtein conformationen_HK
dc.subjectSerum proteinen_HK
dc.subjectStability constanten_HK
dc.titleN-lobe versus C-lobe complexation of bismuth by human transferrinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0264-6021&volume=337&spage=105&epage=111&date=1999&atitle=N-lobe+versus+C-lobe+complexation+of+bismuth+by+human+transferrinen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1042/0264-6021:3370105en_HK
dc.identifier.pmid9854031-
dc.identifier.pmcidPMC1219942-
dc.identifier.scopuseid_2-s2.0-0032952724en_HK
dc.identifier.hkuros43989en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032952724&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume337en_HK
dc.identifier.issue1en_HK
dc.identifier.spage105en_HK
dc.identifier.epage111en_HK
dc.identifier.isiWOS:000078370600015-
dc.publisher.placeUnited Kingdomen_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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