'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.
Hoffmann
A
A
Department of Molecular Biology, GBF - Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany.
Nimtz
M
M
Getzlaff
R
R
Conradt
H S
HS
D000595:Amino Acid Sequence; D001212:Asialoglycoproteins / Q000134:cerebrospinal fluid* / Q000737:chemistry; D002240:Carbohydrate Sequence; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000032:analysis; D011134:Polysaccharides / Q000032:analysis; D014168:Transferrin / Q000031:analogs & derivatives* / Q000134:cerebrospinal fluid / Q000737:chemistry
D001212:Asialoglycoproteins; D009844:Oligosaccharides; D011134:Polysaccharides; D014168:Transferrin; C017031:asialotransferrins