Proteomics

Dataset Information

0

IgA deglycosylation to identify glycosylation sites


ABSTRACT: In order to provide information on the peptide sequence of the IgA glycopeptides, a proteomics analysis was run on LC-MS/MS data of N-glycosidase F-digested IgA samples, in which the N-glycans had been released. The samples included IgA (isolated) from: 1) the saliva samples from two healthy donors, 2) a pooled-plasma standard from a minimum of 20 human donors (VisuCon-F Frozen Normal Control Plasma; Affinity Biologicals, Ancaster, Canada), 3) 10 μg of a human plasma-derived IgA standard (Lee Biosolutions, Maryland Heights, MO), and 4) a human colostrum-derived SIgA standard (Athens Research and Technology, Athens, GA).

INSTRUMENT(S): maXis

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma, Colostrum, Saliva

SUBMITTER: Noortje de Haan  

LAB HEAD: Manfred Wuhrer

PROVIDER: PXD011228 | Pride | 2018-11-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
37787_A05_PNGaseF_salR.mgf Mgf
37787_B05_PNGaseF_salA.mgf Mgf
37787_C05_PNGaseF_Vis.mgf Mgf
37787_D05_PNGaseF_IgAstd.mgf Mgf
37787_E05_PNGaseF_SIgAstd.mgf Mgf
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Publications

Comparative Glycomics of Immunoglobulin A and G From Saliva and Plasma Reveals Biomarker Potential.

Plomp Rosina R   de Haan Noortje N   Bondt Albert A   Murli Jayshri J   Dotz Viktoria V   Wuhrer Manfred M  

Frontiers in immunology 20181023


The <i>N</i>-glycosylation of immunoglobulin (Ig) G, the major antibody in the circulation of human adults, is well known for its influence on antibody effector functions and its alterations with various diseases. In contrast, knowledge on the role of glycans attached to IgA, which is a key immune defense agent in secretions, is very scarce. In this study we aimed to characterize the glycosylation of salivary (secretory) IgA, including the IgA joining chain (JC), and secretory component (SC) and  ...[more]

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