| dc.contributor.author |
Argyri, K |
en |
| dc.contributor.author |
Tako, E |
en |
| dc.contributor.author |
Miller, DD |
en |
| dc.contributor.author |
Glahn, RP |
en |
| dc.contributor.author |
Komaitis, M |
en |
| dc.contributor.author |
Kapsokefalou, M |
en |
| dc.date.accessioned |
2014-06-06T06:49:28Z |
|
| dc.date.available |
2014-06-06T06:49:28Z |
|
| dc.date.issued |
2009 |
en |
| dc.identifier.issn |
00218561 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1021/jf802877n |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4611 |
|
| dc.subject |
Caco-2 cell cultures |
en |
| dc.subject |
Dialysis |
en |
| dc.subject |
Gel filtration |
en |
| dc.subject |
Iron bioavailability |
en |
| dc.subject |
Milk peptides |
en |
| dc.subject.other |
amino acid |
en |
| dc.subject.other |
cation transport protein |
en |
| dc.subject.other |
iron |
en |
| dc.subject.other |
milk protein |
en |
| dc.subject.other |
pepsin A |
en |
| dc.subject.other |
peptide |
en |
| dc.subject.other |
solute carrier family 11 (proton coupled divalent metal ion transporters), member 2 |
en |
| dc.subject.other |
solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2 |
en |
| dc.subject.other |
water |
en |
| dc.subject.other |
animal |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
cell strain CACO 2 |
en |
| dc.subject.other |
chemistry |
en |
| dc.subject.other |
digestion |
en |
| dc.subject.other |
drug effect |
en |
| dc.subject.other |
fractionation |
en |
| dc.subject.other |
gene expression |
en |
| dc.subject.other |
genetics |
en |
| dc.subject.other |
human |
en |
| dc.subject.other |
in vitro study |
en |
| dc.subject.other |
metabolism |
en |
| dc.subject.other |
milk |
en |
| dc.subject.other |
solubility |
en |
| dc.subject.other |
Amino Acids |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Caco-2 Cells |
en |
| dc.subject.other |
Cation Transport Proteins |
en |
| dc.subject.other |
Chemical Fractionation |
en |
| dc.subject.other |
Digestion |
en |
| dc.subject.other |
Gene Expression |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Iron |
en |
| dc.subject.other |
Milk |
en |
| dc.subject.other |
Milk Proteins |
en |
| dc.subject.other |
Pepsin A |
en |
| dc.subject.other |
Peptides |
en |
| dc.subject.other |
Solubility |
en |
| dc.subject.other |
Water |
en |
| dc.title |
Milk peptides increase iron dialyzability in water but do not affect DMT-1 expression in Caco-2 cells |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1021/jf802877n |
en |
| heal.publicationDate |
2009 |
en |
| heal.abstract |
In vitro digestion of milk produces peptide fractions that enhance iron uptake by Caco-2 cells. The objectives of this study were to investigate whether these fractions (a) exert their effect by increasing relative gene expression of DMT-1 in Caco-2 cells and (b) enhance iron dialyzability when added in meals. Two milk peptide fractions that solubilize iron were isolated by Sephadex G-25 gel filtration of a milk digest. These peptide fractions did not affect relative gene expression of DMT-1 when incubated with Caco-2 cells for 2 or 48 h. Dialyzability was measured after in vitro simulated gastric and pancreatic digestion. Both peptide fractions enhanced the dialyzability of iron from ferric chloride added to PIPES buffer, but had no effect on dialyzability from milk or a vegetable or fruit meal after in vitro simulated gastric and pancreatic digestion. However, dialyzability from milk was enhanced by the addition of a more concentrated lyophilized peptide fraction. © 2009 American Chemical Society. |
en |
| heal.journalName |
Journal of Agricultural and Food Chemistry |
en |
| dc.identifier.issue |
4 |
en |
| dc.identifier.volume |
57 |
en |
| dc.identifier.doi |
10.1021/jf802877n |
en |
| dc.identifier.spage |
1538 |
en |
| dc.identifier.epage |
1543 |
en |