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- Publisher Website: 10.1021/jf052086r
- Scopus: eid_2-s2.0-33644506769
- PMID: 16417320
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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
Title | Study of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering |
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Authors | |
Keywords | Buckwheat globulin Fagopyrum esculentum Moench Laser light scattering Quasielastic light scattering Thermal aggregation |
Issue Date | 2006 |
Publisher | American 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/178930 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.114 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, SM | en_US |
dc.contributor.author | Ma, CY | en_US |
dc.date.accessioned | 2012-12-19T09:50:48Z | - |
dc.date.available | 2012-12-19T09:50:48Z | - |
dc.date.issued | 2006 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 2006, v. 54 n. 2, p. 554-561 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178930 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau | en_US |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_US |
dc.subject | Buckwheat globulin | - |
dc.subject | Fagopyrum esculentum Moench | - |
dc.subject | Laser light scattering | - |
dc.subject | Quasielastic light scattering | - |
dc.subject | Thermal aggregation | - |
dc.subject.mesh | Chemistry, Physical | en_US |
dc.subject.mesh | Chromatography, Gel | en_US |
dc.subject.mesh | Ethylmaleimide - Pharmacology | en_US |
dc.subject.mesh | Fagopyrum - Chemistry | en_US |
dc.subject.mesh | Globulins - Chemistry | en_US |
dc.subject.mesh | Hot Temperature | en_US |
dc.subject.mesh | Light | en_US |
dc.subject.mesh | Molecular Weight | en_US |
dc.subject.mesh | Physicochemical Phenomena | en_US |
dc.subject.mesh | Protein Conformation | en_US |
dc.subject.mesh | Protein Denaturation | en_US |
dc.subject.mesh | Scattering, Radiation | en_US |
dc.title | Study of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_US |
dc.identifier.authority | Ma, CY=rp00759 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1021/jf052086r | en_US |
dc.identifier.pmid | 16417320 | - |
dc.identifier.scopus | eid_2-s2.0-33644506769 | en_US |
dc.identifier.hkuros | 115302 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-33644506769&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 54 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 554 | en_US |
dc.identifier.epage | 561 | en_US |
dc.identifier.isi | WOS:000234867400043 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Choi, SM=8873744400 | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.issnl | 0021-8561 | - |