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Glycoproteomic characterization of recombinant mouse α-dystroglycan.
- Source :
-
Glycobiology . May2012, Vol. 22 Issue 5, p662-675. 14p. - Publication Year :
- 2012
-
Abstract
- α-Dystroglycan (DG) is a key component of the dystrophin–glycoprotein complex. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy. Unusually α-DG has previously been demonstrated to be modified with both O-N-acetylgalactosamine and O-mannose initiated glycans. In the present study, Fc-tagged recombinant mouse α-DG was expressed and purified from human embryonic kidney 293T cells. α-DG glycopeptides were characterized by glycoproteomic strategies using both nano-liquid chromatography matrix-assisted laser desorption ionization and electrospray tandem mass spectrometry. A total of 14 different peptide sequences and 38 glycopeptides were identified which displayed heterogeneous O-glycosylation. These data provide new insights into the complex domain-specific O-glycosylation of α-DG. [ABSTRACT FROM PUBLISHER]
Details
- Language :
- English
- ISSN :
- 09596658
- Volume :
- 22
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Glycobiology
- Publication Type :
- Academic Journal
- Accession number :
- 73911251
- Full Text :
- https://doi.org/10.1093/glycob/cws002