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Article: Equilibrium dialysis of metal-serum albumin (II) - Allosteric effect in Ni(II)-serum albumin systems

TitleEquilibrium dialysis of metal-serum albumin (II) - Allosteric effect in Ni(II)-serum albumin systems
Authors
KeywordsAllosteric Effect
Equilibrium Dialysis
Ni(Ii)-Serum Albumin
Successive Stability Constants
Issue Date1997
PublisherScience in China Press. The Journal's web site is located at http://219.238.6.200/journal?code=04
Citation
Science In China, Series B: Chemistry, 1997, v. 40 n. 2, p. 122-127 How to Cite?
AbstractDetailed studies were carried out on equilibrium dialysis of the binding of Ni 2+ ion to human serum albumin (HSA) and bovine serum albumin (BSA). The successive stability constants were obtained by the least-squares fitting. The eight binding sites found for both Ni(II)-HSA and Ni(II)-BSA systems can be divided into two different sets; and for both systems, there exist two identical prior binding sites where the bound Ni 2+ ions can be considered as allosteric effectors, which induce the allosteric effect in accordance with the model proposed by Monod et al. As indicated by allosteric parameters, the ability of R-state to bind Ni 2+ ions is ca. 100 times as much as that of T-state, and the conformation of HSA is markedly tenser than that of BSA.
Persistent Identifierhttp://hdl.handle.net/10722/167397
ISSN
2011 Impact Factor: 1.199
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHu, Xen_US
dc.contributor.authorSong, Zen_US
dc.contributor.authorSu, Xen_US
dc.contributor.authorOuyang, Den_US
dc.contributor.authorHuang, Jen_US
dc.contributor.authorZhou, Yen_US
dc.date.accessioned2012-10-08T03:06:28Z-
dc.date.available2012-10-08T03:06:28Z-
dc.date.issued1997en_US
dc.identifier.citationScience In China, Series B: Chemistry, 1997, v. 40 n. 2, p. 122-127en_US
dc.identifier.issn1006-9291en_US
dc.identifier.urihttp://hdl.handle.net/10722/167397-
dc.description.abstractDetailed studies were carried out on equilibrium dialysis of the binding of Ni 2+ ion to human serum albumin (HSA) and bovine serum albumin (BSA). The successive stability constants were obtained by the least-squares fitting. The eight binding sites found for both Ni(II)-HSA and Ni(II)-BSA systems can be divided into two different sets; and for both systems, there exist two identical prior binding sites where the bound Ni 2+ ions can be considered as allosteric effectors, which induce the allosteric effect in accordance with the model proposed by Monod et al. As indicated by allosteric parameters, the ability of R-state to bind Ni 2+ ions is ca. 100 times as much as that of T-state, and the conformation of HSA is markedly tenser than that of BSA.en_US
dc.languageengen_US
dc.publisherScience in China Press. The Journal's web site is located at http://219.238.6.200/journal?code=04en_US
dc.relation.ispartofScience in China, Series B: Chemistryen_US
dc.subjectAllosteric Effecten_US
dc.subjectEquilibrium Dialysisen_US
dc.subjectNi(Ii)-Serum Albuminen_US
dc.subjectSuccessive Stability Constantsen_US
dc.titleEquilibrium dialysis of metal-serum albumin (II) - Allosteric effect in Ni(II)-serum albumin systemsen_US
dc.typeArticleen_US
dc.identifier.emailHuang, J:jshuang@hkucc.hku.hken_US
dc.identifier.authorityHuang, J=rp00709en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/BF02876402-
dc.identifier.scopuseid_2-s2.0-0010352176en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0010352176&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume40en_US
dc.identifier.issue2en_US
dc.identifier.spage122en_US
dc.identifier.epage127en_US
dc.identifier.isiWOS:A1997WN35700002-
dc.publisher.placeChinaen_US
dc.identifier.scopusauthoridHu, X=7404709756en_US
dc.identifier.scopusauthoridSong, Z=55204311400en_US
dc.identifier.scopusauthoridSu, X=7402182042en_US
dc.identifier.scopusauthoridOuyang, D=7003347082en_US
dc.identifier.scopusauthoridHuang, J=7407192639en_US
dc.identifier.scopusauthoridZhou, Y=8047648700en_US

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