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Kapcsolat
Tissue-specific glycosylation at the glycopeptide level |
Tartalom: | http://real.mtak.hu/30046/ |
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Archívum: | MTA Könyvtár |
Gyűjtemény: |
Status = Published
Type = Article |
Cím: |
Tissue-specific glycosylation at the glycopeptide level
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Létrehozó: |
Medzihradszky F., Katalin
Kaasik, K.
Chalkley, RJ.
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Dátum: |
2015
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Téma: |
QH301 Biology / biológia
QH3011 Biochemistry / biokémia
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Tartalmi leírás: |
This manuscript describes the enrichment and mass spectrometric analysis of intact glycopeptides from mouse liver, which yielded site-specific N- and O-glycosylation data for ?130 proteins. Incorporation of different sialic acid variants in both N- and O-linked glycans was observed, and the importance of using both collisional activation and electron transfer dissociation for glycopeptide analysis was illustrated. The N-glycan structures of predicted lysosomal, endoplasmic reticulum (ER), secreted and transmembrane proteins were compared. The data suggest that protein N-glycosylation differs depending on cellular location. The glycosylation patterns of several mouse liver and mouse brain glycopeptides were compared. Tissue-specific differences in glycosylation were observed between sites within the same protein: Some sites displayed a similar spectrum of glycan structures in both tissues, whereas for others no overlap was observed. We present comparative brain/liver glycosylation data on 50 N-glycosylation sites from 34 proteins and 13 O-glycosylation sites from seven proteins. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
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Típus: |
Article
PeerReviewed
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Formátum: |
text
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Azonosító: |
Medzihradszky F., Katalin and Kaasik, K. and Chalkley, RJ. (2015) Tissue-specific glycosylation at the glycopeptide level. MOLECULAR & CELLULAR PROTEOMICS, 14 (8). pp. 2103-2110. ISSN 1535-9476
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Kapcsolat: |
https://dx.doi.org/10.1074/mcp.M115.050393
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