- Abstract:
-
All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate and used it to rapidly isolate IgG from plasma of 2298 individuals from three isolated human populations. N-glycans were released by PNGase F, labeled with 2-aminobenzamide and analyzed by hydrophi...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/mcp.m111.010090
-
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- Journal:
- Molecular and cellular proteomics : MCP
- Volume:
- 10
- Issue:
- 10
- Pages:
- M111.010090
- Publication date:
- 2011-10-05
- DOI:
- EISSN:
-
1535-9484
- ISSN:
-
1535-9476
- URN:
-
uuid:d11f6fd2-4cb0-46d8-a462-c8fa7bc43eb5
- Source identifiers:
-
151219
- Local pid:
- pubs:151219
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations.
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