Abstract
Human milk is a rich source of bioactive proteins that support the early growth and development of the newborn. Although the major components of the protein fraction in human milk have been studied, the expression and relative abundance of minor components have received limited attention. We examined the expression of low-abundance proteins in the whey fraction of human milk and their dynamic changes over a twelve-month lactation period. The low-abundance proteins were enriched by ProteoMiner beads, and protein identification was performed by liquid chromatography tandem mass spectrometry. One hundred and fifteen proteins were identified, thirty-eight of which have not been previously reported in human colostrum or milk. We also for the first time described differences in protein patterns among the low-abundance proteins during lactation. These results enhance our knowledge about the complexity of the human milk proteome, which constitutes part of the advantages to the breast-fed infant.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1746-1754 |
| Number of pages | 9 |
| Journal | Journal of Proteome Research |
| Volume | 10 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 1 2011 |
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Keywords
- human milk
- LC-MS/MS
- protein
- proteomics
- whey
ASJC Scopus subject areas
- Biochemistry
- Chemistry(all)
Cite this
Proteomic characterization of human milk whey proteins during a twelve-month lactation period. / Liao, Yalin; Alvarado, Rudy; Phinney, Brett; Lönnerdal, Bo.
In: Journal of Proteome Research, Vol. 10, No. 4, 01.04.2011, p. 1746-1754.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteomic characterization of human milk whey proteins during a twelve-month lactation period
AU - Liao, Yalin
AU - Alvarado, Rudy
AU - Phinney, Brett
AU - Lönnerdal, Bo
PY - 2011/4/1
Y1 - 2011/4/1
N2 - Human milk is a rich source of bioactive proteins that support the early growth and development of the newborn. Although the major components of the protein fraction in human milk have been studied, the expression and relative abundance of minor components have received limited attention. We examined the expression of low-abundance proteins in the whey fraction of human milk and their dynamic changes over a twelve-month lactation period. The low-abundance proteins were enriched by ProteoMiner beads, and protein identification was performed by liquid chromatography tandem mass spectrometry. One hundred and fifteen proteins were identified, thirty-eight of which have not been previously reported in human colostrum or milk. We also for the first time described differences in protein patterns among the low-abundance proteins during lactation. These results enhance our knowledge about the complexity of the human milk proteome, which constitutes part of the advantages to the breast-fed infant.
AB - Human milk is a rich source of bioactive proteins that support the early growth and development of the newborn. Although the major components of the protein fraction in human milk have been studied, the expression and relative abundance of minor components have received limited attention. We examined the expression of low-abundance proteins in the whey fraction of human milk and their dynamic changes over a twelve-month lactation period. The low-abundance proteins were enriched by ProteoMiner beads, and protein identification was performed by liquid chromatography tandem mass spectrometry. One hundred and fifteen proteins were identified, thirty-eight of which have not been previously reported in human colostrum or milk. We also for the first time described differences in protein patterns among the low-abundance proteins during lactation. These results enhance our knowledge about the complexity of the human milk proteome, which constitutes part of the advantages to the breast-fed infant.
KW - human milk
KW - LC-MS/MS
KW - protein
KW - proteomics
KW - whey
UR - http://www.scopus.com/inward/record.url?scp=79953697144&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79953697144&partnerID=8YFLogxK
U2 - 10.1021/pr101028k
DO - 10.1021/pr101028k
M3 - Article
C2 - 21361340
AN - SCOPUS:79953697144
VL - 10
SP - 1746
EP - 1754
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 4
ER -