dc.contributor.author | Rytkonen, J | |
dc.contributor.author | Valkonen, KH | |
dc.contributor.author | Virtanen, V | |
dc.contributor.author | Foxwell, RA | |
dc.contributor.author | Kyd, JM | |
dc.contributor.author | Cripps, AW | |
dc.contributor.author | Karttunen, TJ | |
dc.date.accessioned | 2017-05-03T14:29:37Z | |
dc.date.available | 2017-05-03T14:29:37Z | |
dc.date.issued | 2006 | |
dc.date.modified | 2009-09-04T06:01:56Z | |
dc.identifier.issn | 0021-8561 | |
dc.identifier.doi | 10.1021/jf052309d | |
dc.identifier.uri | http://hdl.handle.net/10072/11341 | |
dc.description.abstract | The 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.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | American Chemical Society | |
dc.publisher.place | United States of America | |
dc.publisher.uri | http://pubs3.acs.org/acs/journals/toc.page?incoden=jafcau | |
dc.relation.ispartofstudentpublication | N | |
dc.relation.ispartofpagefrom | 1500 | |
dc.relation.ispartofpageto | 1507 | |
dc.relation.ispartofedition | 2006 | |
dc.relation.ispartofjournal | Journal of Agricriculture and Food Chemistry | |
dc.relation.ispartofvolume | 54 | |
dc.rights.retention | Y | |
dc.subject.fieldofresearch | Chemical sciences | |
dc.subject.fieldofresearch | Agricultural, veterinary and food sciences | |
dc.subject.fieldofresearch | Engineering | |
dc.subject.fieldofresearchcode | 34 | |
dc.subject.fieldofresearchcode | 30 | |
dc.subject.fieldofresearchcode | 40 | |
dc.title | Enterocyte and M-Cell Transport of Native and Heat-Denatured Bovine β-Lactoglobulin: Significance of Heat Denaturation | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - 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.issued | 2006 | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | Cripps, Allan W. | |