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Article: Thermal stability of β-lactoglobulins A and B: Effect of SDS, urea, cysteine and N-ethylmaleimide

TitleThermal stability of β-lactoglobulins A and B: Effect of SDS, urea, cysteine and N-ethylmaleimide
Authors
Keywordsβ-Lactoglobulin
Denaturation
Differential scanning calorimetry
FTIR
Infrared spectroscopy
Issue Date2004
PublisherCambridge University Press. The Journal's web site is located at http://journals.cambridge.org/action/displayJournal?jid=DAR
Citation
Journal Of Dairy Research, 2004, v. 71 n. 2, p. 207-215 How to Cite?
AbstractFourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of β-lactoglobulin A and B in the presence of sodium dodecyl sulphate (SDS), N-ethylmaleimide (NEM), urea and cysteine. An increase in the thermal stabilities of both proteins was noted in the presence of 10 mM-SDS. In the presence of 50 mM-SDS, there was extensive denaturation of both variants. In general, the β-strand/β-sheet regions in the secondary structure of both variants were very susceptible to denaturation by SDS and cysteine, suggesting that these regions may be held by hydrophobic and disulphide bonds. At ambient temperature and physiological pH, a notable difference was observed in the 1636 and 1627 cm -1 regions of the FTIR spectra of the two β-Ig variants. The results suggest possible differences in the nature of the β-sheet/β-strand distribution/content of the two proteins. Urea and NEM at a concentration of 50 mM, had little effect on the secondary structure and denaturation of both variants. New findings are presented which further indicate that although the β-Ig B variant showed greater thermal stability than the A variant in all the cases studied, its denaturation temperature and secondary structure were affected to a greater extent by the protein perturbants than ß-Ig A.
Persistent Identifierhttp://hdl.handle.net/10722/42021
ISSN
2015 Impact Factor: 1.5
2015 SCImago Journal Rankings: 0.682
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorBoye, JIen_HK
dc.contributor.authorMa, CYen_HK
dc.contributor.authorIsmail, Aen_HK
dc.date.accessioned2007-01-08T02:27:08Z-
dc.date.available2007-01-08T02:27:08Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Dairy Research, 2004, v. 71 n. 2, p. 207-215en_HK
dc.identifier.issn0022-0299en_HK
dc.identifier.urihttp://hdl.handle.net/10722/42021-
dc.description.abstractFourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of β-lactoglobulin A and B in the presence of sodium dodecyl sulphate (SDS), N-ethylmaleimide (NEM), urea and cysteine. An increase in the thermal stabilities of both proteins was noted in the presence of 10 mM-SDS. In the presence of 50 mM-SDS, there was extensive denaturation of both variants. In general, the β-strand/β-sheet regions in the secondary structure of both variants were very susceptible to denaturation by SDS and cysteine, suggesting that these regions may be held by hydrophobic and disulphide bonds. At ambient temperature and physiological pH, a notable difference was observed in the 1636 and 1627 cm -1 regions of the FTIR spectra of the two β-Ig variants. The results suggest possible differences in the nature of the β-sheet/β-strand distribution/content of the two proteins. Urea and NEM at a concentration of 50 mM, had little effect on the secondary structure and denaturation of both variants. New findings are presented which further indicate that although the β-Ig B variant showed greater thermal stability than the A variant in all the cases studied, its denaturation temperature and secondary structure were affected to a greater extent by the protein perturbants than ß-Ig A.en_HK
dc.format.extent1048974 bytes-
dc.format.extent1916 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypetext/plain-
dc.languageengen_HK
dc.publisherCambridge University Press. The Journal's web site is located at http://journals.cambridge.org/action/displayJournal?jid=DARen_HK
dc.relation.ispartofJournal of Dairy Researchen_HK
dc.rightsJournal of Dairy Research. Copyright © Cambridge University Press.en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectβ-Lactoglobulinen_HK
dc.subjectDenaturationen_HK
dc.subjectDifferential scanning calorimetryen_HK
dc.subjectFTIRen_HK
dc.subjectInfrared spectroscopyen_HK
dc.subject.meshCysteine - pharmacologyen_HK
dc.subject.meshEthylmaleimide - pharmacologyen_HK
dc.subject.meshHeaten_HK
dc.subject.meshLactoglobulins - chemistryen_HK
dc.subject.meshSodium dodecyl sulfate - pharmacologyen_HK
dc.titleThermal stability of β-lactoglobulins A and B: Effect of SDS, urea, cysteine and N-ethylmaleimideen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-0299&volume=71&issue=2&spage=207&epage=215&date=2004&atitle=Thermal+stability+of+[beta]-lactoglobulins+A+and+B:+effect+of+SDS,+urea,+cysteine+and+N-ethylmaleimideen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1017/S0022029904000184en_HK
dc.identifier.pmid15190950-
dc.identifier.scopuseid_2-s2.0-2542555974en_HK
dc.identifier.hkuros115484-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2542555974&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume71en_HK
dc.identifier.issue2en_HK
dc.identifier.spage207en_HK
dc.identifier.epage215en_HK
dc.identifier.isiWOS:000221715300012-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridBoye, JI=7003390065en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridIsmail, A=7201548364en_HK

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