Proteomic characterization of human milk whey proteins during a twelve-month lactation period
Yalin Liao, Rudy Alvarado, Brett Phinney, Bo Lönnerdal
Endocrinology, Diabetes, and Metabolism
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.
Journal of Proteome Research
https://doi.org/10.1021/pr101028k
Proteome
Tandem Mass Spectrometry
Whey Proteins
LC-MS/MS
Liao, Y., Alvarado, R., Phinney, B., & Lönnerdal, B. (2011). Proteomic characterization of human milk whey proteins during a twelve-month lactation period. Journal of Proteome Research, 10(4), 1746-1754. https://doi.org/10.1021/pr101028k
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.
Liao, Y, Alvarado, R, Phinney, B & Lönnerdal, B 2011, 'Proteomic characterization of human milk whey proteins during a twelve-month lactation period', Journal of Proteome Research, vol. 10, no. 4, pp. 1746-1754. https://doi.org/10.1021/pr101028k
Liao Y, Alvarado R, Phinney B, Lönnerdal B. Proteomic characterization of human milk whey proteins during a twelve-month lactation period. Journal of Proteome Research. 2011 Apr 1;10(4):1746-1754. https://doi.org/10.1021/pr101028k
Liao, Yalin ; Alvarado, Rudy ; Phinney, Brett ; Lönnerdal, Bo. / Proteomic characterization of human milk whey proteins during a twelve-month lactation period. In: Journal of Proteome Research. 2011 ; Vol. 10, No. 4. pp. 1746-1754.
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title = "Proteomic characterization of human milk whey proteins during a twelve-month lactation period",
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.",
keywords = "human milk, LC-MS/MS, protein, proteomics, whey",
author = "Yalin Liao and Rudy Alvarado and Brett Phinney and Bo L{\"o}nnerdal",
doi = "10.1021/pr101028k",
journal = "Journal of Proteome Research",
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
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
U2 - 10.1021/pr101028k
DO - 10.1021/pr101028k
JO - Journal of Proteome Research
JF - Journal of Proteome Research
10.1021/pr101028k