Baum F, Fedorova M, Ebner J, Hoffmann R, Pischetsrieder M (2013)
Publication Type: Journal article
Publication year: 2013
Publisher: American Chemical Society
Book Volume: 12
Pages Range: 5447-5462
URI: http://pubs.acs.org/articlesonrequest/AOR-2X56c2EdZb76MC49EC6C
DOI: 10.1021/pr4003273
Milk is an excellent source of bioactive peptides. However, the composition of the native milk peptidome has only been partially elucidated. The present study applied matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) directly or after prefractionation of the milk peptides by reverse-phase high-performance liquid chromatography (RP-HPLC) or OFFGEL fractionation for the comprehensive analysis of the peptide profile of raw milk. The peptide sequences were determined by MALDI-TOF/TOF or nano-ultra-performance liquid chromatography-nanoelectrospray ionization-LTQ-Orbitrap-MS. Direct MALDI-TOF-MS analysis led to the assignment of 57 peptides. Prefractionation by both complementary methods led to the assignment of another 191 peptides. Most peptides originate from α
APA:
Baum, F., Fedorova, M., Ebner, J., Hoffmann, R., & Pischetsrieder, M. (2013). Analysis of the endogenous peptide profile of milk: Identification of 248 mainly casein-derived peptides. Journal of Proteome Research, 12, 5447-5462. https://doi.org/10.1021/pr4003273
MLA:
Baum, Florian, et al. "Analysis of the endogenous peptide profile of milk: Identification of 248 mainly casein-derived peptides." Journal of Proteome Research 12 (2013): 5447-5462.
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