Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/202062
Type: Artigo de periódico
Title: Metal Ions Bound To The Human Milk Immunoglobulin A: Metalloproteomic Approach.
Author: Pozzi, Carla Mariane Costa
Braga, Camila Pereira
Vieira, José Cavalcante Souza
Cavecci, Bruna
Vitor de Queiroz, João
de Souza Barbosa, Herbert
Arruda, Marco Aurelio Zezzi
Gozzo, Fabio Cesar
Padilha, Pedro de Magalhães
Abstract: The presence of calcium, iron, and zinc bound to human milk secretory IgA (sIgA) was investigated. The sIgA components were first separated by two-dimensional polyacrylamide gel electrophoresis and then identified by electrospray ionization-tandem mass spectrometry (ESI MS MS). The metal ions were detected by flame atomic absorption spectrometry after acid mineralization of the spots. The results showed eight protein spots corresponding to the IgA heavy chain constant region. Another spot was identified as the transmembrane secretory component. Calcium was bound to both the transmembrane component and the heavy chain constant region, while zinc was bound to the heavy chain constant region and iron was not bound with the identified proteins. The association of a metal ion with a protein is important for a number of reasons, and therefore, the findings of the present study may lead to a better understanding of the mechanisms of action and of additional roles that sIgA and its components play in human milk.
Subject: Electrospray Ionization–tandem Mass Spectrometry
Flame Atomic Absorption Spectrometry
Human Milk
Metalloproteomics
Secretory Iga
Two-dimensional Electrophoresis
Rights: fechado
Identifier DOI: 10.1016/j.foodchem.2014.06.040
Address: http://www.ncbi.nlm.nih.gov/pubmed/25053085
Date Issue: 2015
Appears in Collections:Unicamp - Artigos e Outros Documentos

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