Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/85241
Type: Artigo de periódico
Title: Metal Ions Bound To The Human Milk Immunoglobulin A: Metalloproteomic Approach
Author: Pozzi C.M.C.
Braga C.P.
Vieira J.C.S.
Cavecci B.
Queiroz J.V.
Barbosa H.
Arruda M.A.Z.
Gozzo F.C.
Padilha P.D.M.
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. © 2014 Elsevier Ltd. All rights reserved.
Editor: Elsevier Ltd
Rights: fechado
Identifier DOI: 10.1016/j.foodchem.2014.06.040
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84903827597&partnerID=40&md5=c778e5bf2ff34832c87f1a70cc249aeb
Date Issue: 2015
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
2-s2.0-84903827597.pdf533.64 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.