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Article: Study of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering

TitleStudy of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2006, v. 54 n. 2, p. 554-561 How to Cite?
AbstractThe heat-induced aggregation of common buckwheat (Fagopyrum esculetum Moench) globulin (BWG) was studied using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and quasielastic light scattering (QELS). The unheated BWG was found to exist mainly as a hexamer, with an estimated weight-average molecular weight (Mw) of 342 000, close to that deduced from the genomic cloned data of 13S buckwheat globulin. The QELS data predicted that the hexamer exists as two annular trimeric rings (diameter ∼ 10.8 nm) placed on top of each other, forming an oblate cylinder (height ∼ 9.1 nm). Upon heating, hexamers and trimers were dissociated and then associated to form extended small aggregates, finally forming compact, large macroaggregates. N-Ethylmaleimide would favor macroaggregate formation and increased the molar masses and hydrodynamic radii of the soluble aggregates, suggesting a different aggregation process in the presence of the sulfhydryl-blocking agent. A plot of log hydrodynamic radius versus log molar mass showed changes in the slope during heat treatment, suggesting conformational transformation in the heat-denatured and aggregated BWG molecules. © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/178930
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChoi, SMen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:50:48Z-
dc.date.available2012-12-19T09:50:48Z-
dc.date.issued2006en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2006, v. 54 n. 2, p. 554-561en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178930-
dc.description.abstractThe heat-induced aggregation of common buckwheat (Fagopyrum esculetum Moench) globulin (BWG) was studied using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and quasielastic light scattering (QELS). The unheated BWG was found to exist mainly as a hexamer, with an estimated weight-average molecular weight (Mw) of 342 000, close to that deduced from the genomic cloned data of 13S buckwheat globulin. The QELS data predicted that the hexamer exists as two annular trimeric rings (diameter ∼ 10.8 nm) placed on top of each other, forming an oblate cylinder (height ∼ 9.1 nm). Upon heating, hexamers and trimers were dissociated and then associated to form extended small aggregates, finally forming compact, large macroaggregates. N-Ethylmaleimide would favor macroaggregate formation and increased the molar masses and hydrodynamic radii of the soluble aggregates, suggesting a different aggregation process in the presence of the sulfhydryl-blocking agent. A plot of log hydrodynamic radius versus log molar mass showed changes in the slope during heat treatment, suggesting conformational transformation in the heat-denatured and aggregated BWG molecules. © 2006 American Chemical Society.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_US
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_US
dc.subject.meshChemistry, Physicalen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshEthylmaleimide - Pharmacologyen_US
dc.subject.meshFagopyrum - Chemistryen_US
dc.subject.meshGlobulins - Chemistryen_US
dc.subject.meshHot Temperatureen_US
dc.subject.meshLighten_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshPhysicochemical Phenomenaen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Denaturationen_US
dc.subject.meshScattering, Radiationen_US
dc.titleStudy of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scatteringen_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/jf052086ren_US
dc.identifier.pmid16417320-
dc.identifier.scopuseid_2-s2.0-33644506769en_US
dc.identifier.hkuros115302-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33644506769&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume54en_US
dc.identifier.issue2en_US
dc.identifier.spage554en_US
dc.identifier.epage561en_US
dc.identifier.isiWOS:000234867400043-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChoi, SM=8873744400en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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