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- W1975975363 abstract "We identified several low-abundance proteins of bovine colostrum and mature milk using the immunoabsorption technique and two-dimensional electrophoresis (2-DE) followed by microsequencing and mass spectrometry. Two major milk proteins, β-casein and immunoglobulin G (IgG), were effectively removed from the milk using immunoabsorbents. Milk samples before and after immunoabsorption were separated by 2-DE. Protein identification of the spots on 2-DE was performed by either gel comparison, microsequencing, matrix-assisted laser desorption/ionization-time of flight mass-spectrometry (MALDI-TOF-MS), peptide mass fingerprinting or peptide sequencing using tandem MS by hybrid quadrupole/orthogonal acceleration time of flight-MS (Q-TOF). Significant differences in protein patterns were observed between the low-abundance proteins of colostrum and mature milk. In addition, several low-abundance proteins including fibrinogen β-chain, chitinase 3-like 1, α-antitrypsin, complement C3 α-chain, gelsolin and apolipoprotein H were observed only in colostrum. However, the level of β-casein fragments increased significantly during this lactation period. α-Lactalbumin and β-lactoglobulin as well as some low-abundance proteins including bovine serum albumin, serotransferrin and lactoferrin were identified in both colostral and mature milk. Low-abundance proteins in bovine colostrum may have special physiologic relevance to the health and development of calves early in lactation." @default.
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- W1975975363 date "2002-04-01" @default.
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- W1975975363 title "Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry" @default.
- W1975975363 doi "https://doi.org/10.1002/1522-2683(200204)23:7/8<1153::aid-elps1153>3.0.co;2-y" @default.
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