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dc.contributor.authorRytkonen, J
dc.contributor.authorValkonen, KH
dc.contributor.authorVirtanen, V
dc.contributor.authorFoxwell, RA
dc.contributor.authorKyd, JM
dc.contributor.authorCripps, AW
dc.contributor.authorKarttunen, TJ
dc.date.accessioned2017-05-03T14:29:37Z
dc.date.available2017-05-03T14:29:37Z
dc.date.issued2006
dc.date.modified2009-09-04T06:01:56Z
dc.identifier.issn0021-8561
dc.identifier.doi10.1021/jf052309d
dc.identifier.urihttp://hdl.handle.net/10072/11341
dc.description.abstractThe three-dimensional structure, digestibility, and immunological properties of bovine ߭lactoglobulin (߭lg) are modified by heat treatments used in processing of liquid milk products. Because it is not known if such treatments also modify the intestinal transport properties of ߭lg, the transport of native and heat-denatured bovine ߭lg was investigated in experimental cell models using Caco-2 cells and M cells. Transport of ߭lg labeled with a fluorescent marker was followed with fluorometric measurements, electrophoretic analyses, and fluorescence microscopy. The data show that both cell types transported native ߭lg more efficiently than they did heat-denatured ߭lg. In addition, M cells transported native ߭lg more than Caco-2 cells. Transport of native and heat-denatured ߭lg was transcellular. The electrophoretic data also suggest that heat-denatured ߭lg may have degraded more than native ߭lg during the transport
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.publisher.placeUnited States of America
dc.publisher.urihttp://pubs3.acs.org/acs/journals/toc.page?incoden=jafcau
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom1500
dc.relation.ispartofpageto1507
dc.relation.ispartofedition2006
dc.relation.ispartofjournalJournal of Agricriculture and Food Chemistry
dc.relation.ispartofvolume54
dc.rights.retentionY
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchAgricultural, veterinary and food sciences
dc.subject.fieldofresearchEngineering
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode30
dc.subject.fieldofresearchcode40
dc.titleEnterocyte and M-Cell Transport of Native and Heat-Denatured Bovine β-Lactoglobulin: Significance of Heat Denaturation
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2006 American Chemical Society. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please use the hypertext link to access the journal's website or contact the author for more information. Please refer to the journal for the definitive published version.
gro.date.issued2006
gro.hasfulltextNo Full Text
gro.griffith.authorCripps, Allan W.


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