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Título: | Detection of two minor phosphorylation sites for bovine κ-casein macropeptide by reversed-phase liquid chromatography–tandem mass spectrometry |
Autor: | Hernández-Hernández, Oswaldo CSIC ORCID ; Lebrón-Aguilar, Rosa CSIC ORCID ; Quintanilla-López, Jesús Eduardo CSIC ORCID ; Sanz, M. Luz CSIC ORCID ; Moreno, F. Javier CSIC ORCID | Fecha de publicación: | 2011 | Editor: | American Chemical Society | Citación: | Journal of Agricultural and Food Chemistry 59(20): 10848-10853 (2011) | Resumen: | This work addresses the characterization of phosphopeptides in bovine κ-casein macropeptide by reversed-phase liquid chromatography-electrospray ionization-tandem mass spectrometry (RPLC-ESI-MS2). Two different mass spectrometers, equipped with an ion trap (IT) or a quadrupole time-of-flight (Q-TOF) analyzer, were used to perform an accurate phosphorylation site assignment. A total of 8 phosphopeptides from 26 identified peptides were characterized. MS2 spectra of phosphopeptides were dominated by the neutral loss of a phosphoric acid molecule (H 3PO4) and sufficient informative fragment ions resulting from peptide backbone cleavages enabling the elucidation of the phosphopeptide sequence. A higher number of sequence informative b and y ions were detected using a Q-TOF instead of an IT analyzer. In addition to the well-established phosphorylation sites at Ser149 and Ser127, this study also revealed the presence of two minor phosphorylation sites at Thr 145 and Ser166. These findings indicate that RPLC-ESI-MS2 on a Q-TOF analyzer is a useful technique for identifying low-abundance phosphorylation sites in caseins. © 2011 American Chemical Society. | URI: | http://hdl.handle.net/10261/51628 | DOI: | 10.1021/jf203089n | Identificadores: | doi: 10.1021/jf203089n issn: 0021-8561 e-issn: 1520-5118 |
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