The glycosylation of myeloperoxidase |
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Authors: | Tina Ravnsborg,Gunnar Houen,Peter Hø jrup |
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Affiliation: | 1. Institute of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark;2. Statens Serum Institut, Department of Clinical Biochemistry, Artillerivej 5, DK-2300 Copenhagen, Denmark |
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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. |
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Keywords: | ALL, Acute lymphocytic leukemia AML, Acute myelogenous leukemia DHB, 2,5-dihydroxybenzoic acid FA, Formic acid Fuc, Fucose GlcNAc, N-Acetylglucosamine Hex, Hexose HexNAc, N-Acetylhexosamine MALDI, Matrix assisted laser desorption ionization Man, Mannose MeCN, Acetonitrile MeOH, Methanol MPO, Myeloperoxidase QTOF, Quadropole time of flight Sia, Sialic acid TFA, Trifluoroacetic acid |
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