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- W314528046 abstract "At this present work, the presence of calcium, iron and zinc bound to secretory immunoglobulin A (sIgA) from human milk was investigated. The sIgA components were separated by two-dimensional electrophoresis (2D-PAGE) and they were identified by electrospray ionization mass spectrometry (ESI/MS/MS). A train of eight spots with 5.4<pI<6.5 and a mass of 78 kDa were identified as the Ig alpha-1 chain constant region. Another spot, with pI of 5.8 and a mass of 100 kDa was identified as transmembrane secretory component, also known as the polymeric immunoglobulin receptor (pIgR). The metal ions in the spots were detected by flame atomic absorption spectrometry (FAAS) after acid mineralization of the spots. It was discovered calcium bound to both pIgR and Ig alpha-1 constant region, while zinc was found to be bound to the Ig alpha-1 constant region. The association of a metal ion to a protein (subject of study of metalloproteomics) is important for many reasons and the discoveries of this study can lead to a better understanding of mechanisms of action and additional roles that sIgA and its components have in human milk. Financial support: FAPESP (2011/03291–0)." @default.
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- W314528046 date "2013-04-01" @default.
- W314528046 modified "2023-10-01" @default.
- W314528046 title "Metalloproteomic approach to the determination of calcium, iron and zinc bound to secretory immunoglobulin A in human milk" @default.
- W314528046 doi "https://doi.org/10.1096/fasebj.27.1_supplement.lb141" @default.
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