′Brain-type′ N-glycosylation of asialo-transferrin from human cerebrospinal fluid


Asialo-transferrin from human cerebrospinal fluid was purified to homogeneity. Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins. For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used. The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose. Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.

Language: English   
Format: html   
Type: Dataset /dataset
Subject: Biology and Life Sciences ; biochemical research methods ; biochemistry & molecular biology ;
Keywords: Biochemistry; Bioinformatics; Carbohydrate sequence; Mankind; Cerebrospinal fluid; Sialic acid; N-glycosylation; Sugar chain structure;
Copyright:Copyright. Macquarie University (Biomolecular Frontiers Research Centre), Australia; Proteome Informatics Group (Swiss Institute for Bioinformatics)
Audience: Student   Researcher   Teacher   
Access: Open Access
License:UniCarb-DB is open source platform and an open access resource. The resources published via the platform need to be referenced when used. For example: UniCarb-DB, http://www.unicarb-db.org last accessed: dd/mm/yyyy. with citation

Other Informations:
Source: harvest
Registered Date:2012-10-30 10:47:20.0
Modified Date:2013-05-02 10:08:01.0
The Last Checked Date:2018-01-22 01:18:42.0