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The glycosylation of myeloperoxidase

Authors :
Ravnsborg, Tina
Houen, Gunnar
Højrup, Peter
Source :
BBA - Proteins & Proteomics. Oct2010, Vol. 1804 Issue 10, p2046-2053. 8p.
Publication Year :
2010

Abstract

Abstract: The enzyme myeloperoxidase (MPO) is an important part of the neutrophil immune reaction and can be found in alfa granula. The presence of MPO can be used to distinguish acute myelogenous leukemia from acute lymphocytic leukemia. However, the methods employed to do so, such as flow cytometry and immunohistochemistry rely on antibody recognition, and therefore the characterization of the mature MPO, including post-translational modifications, must be considered as important as epitope mapping. MPO has 5 N-linked glycosylation sites, occupied by both high mannose and complex glycan structures. In this study we utilize intact glycopeptide MSMS analysis for site specific characterization of the glycan structures of MPO from a cancer patient. The identified glycan structures are compared to those of MPO from healthy donors, in order to probe for any potential differences that may have diagnostic use. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
15709639
Volume :
1804
Issue :
10
Database :
Academic Search Index
Journal :
BBA - Proteins & Proteomics
Publication Type :
Academic Journal
Accession number :
53335239
Full Text :
https://doi.org/10.1016/j.bbapap.2010.07.001