Proteomics

Dataset Information

0

Grass carp serum IgM LC-ESI-MS/MS and MALDI-MS


ABSTRACT: Glycosylation represents a major post-translational modification of proteins that can influence their structure and function.Telesot immunoglobulin M (IgM) is an especially important product of the immune system because it is the main Abs in seum and plays a critical role against defense infection. However, little is known regarding site-specific N-glycan characteristics in teleost IgM , LC-ESI-MS/MS was used to analysis deglycopeptides and glycopeptides of grass carp serum IgM, and MALDI-MS was used to analysis released carbohydrates by PNGaseF diestion of grass carp serum IgM.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Ctenopharyngodon Idella

TISSUE(S): Blood Plasma

SUBMITTER: Yiling Su  

LAB HEAD: Hui Geng

PROVIDER: PXD010308 | Pride | 2018-11-29

REPOSITORIES: Pride

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Publications

Site-Specific N-Glycan Characterization of Grass Carp Serum IgM.

Su Yi-Ling YL   Wang Bing B   Hu Meng-Die MD   Cui Zheng-Wei ZW   Wan Jian J   Bai Hao H   Yang Qian Q   Cui Yan-Fang YF   Wan Cui-Hong CH   Xiong Li L   Zhang Yong-An YA   Geng Hui H  

Frontiers in immunology 20181114


Immunoglobulin M (IgM) is the major antibody in teleost fish and plays an important role in humoral adaptive immunity. The N-linked carbohydrates presenting on IgM have been well documented in higher vertebrates, but little is known regarding site-specific N-glycan characteristics in teleost IgM. In order to characterize these site-specific N-glycans, we conducted the first study of the N-glycans of each glycosylation site of the grass carp serum IgM. Among the four glycosylation sites, the Asn-  ...[more]

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