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Proteomic characterization of human milk whey proteins during a twelve‐month lactation period
Author(s) -
Lonnerdal Bo,
Liao Yalin,
Alvarado Rudy,
Phinney Brett
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.104.6
Subject(s) - lactation , period (music) , whey protein , food science , zoology , chemistry , biology , pregnancy , genetics , physics , acoustics
Human milk is a rich source of bioactive proteins that support early growth and development of the newborn. Although the major components of the protein fraction have been studied, the 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 using a Paradigm MG4 HPLC system coupled with a Thermo LTQ ion trap spectrometer. X! Tandem software was set up to search the Uniprot human complete proteome set data base and Scaffold (Proteome Software) was used to validate MS/MS based peptide and protein identifications. One hundred and fifteen proteins were identified, thirty‐eight of which have not been previously reported in human colostrum or milk. Eight functional groups were found: 35% of all proteins are involved in immune function, 17% in cell communication/signal transduction, 16% in metabolism/energy production pathways, 8% in protein metabolism (including translation, folding, trafficking, etc), 5% in cell growth and/or maintenance, 3% in nucleic acid metabolism and 3 % are multifunctional proteins. We also for the first time describe differences in protein patterns among the low‐abundance proteins during lactation. These results enhance our knowledge about the complexity of the human milk proteome and provide suggestions for their physiological significance in the mammary gland and in the breast‐fed infant. (Supported by Mead Johnson Nutrition)