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- W2009764534 abstract "Abstract: The glycoprotein component in rat brain reacting most strongly with Galanthus nivalis agglutinin (GNA) on western blots migrates as an 85-kDa band. GNA identifies mannose-rich oligosaccharides because it is highly specific for terminal α-mannose residues. After purification of this 85-kDa glycoprotein band by chromatography on GNA-agarose and preparative gel electrophoresis, binding of other lectins demonstrated the presence of fucose and a trace of galactose, but no sialic acid. Treatment with N-Glycanase or endoglycosidase H produced a 65-kDa band, indicating that it consisted of about one-fourth N-linked oligomannosidic carbohydrate moieties. High-performance anion-exchange chromatography and fluorescence-assisted carbohydrate electrophoresis indicated that the major carbohydrate moiety is a heptasaccharide with the structure Manα1-6(Manα1-3)Manα1-6(Manα1-3)Manβ1-4Glc-NAcβ1-4GlcNAc (Man5GlcNAc2). Determination of amino acid sequences of peptides produced by endoproteinase digestion demonstrated that this 85-kDa mannose-rich glycoprotein component contained the SHP substrate-1 for phosphotyrosine phosphatases and at least one other member of the signal-regulatory protein (SIRP) family. The unusually high content of oligomannosidic carbohydrate moieties on these receptor-like members of the immunoglobulin superfamily in neural tissue could be of functional significance for intercellular adhesion or signaling." @default.
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- W2009764534 date "2001-12-25" @default.
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- W2009764534 title "Prominent 85-kDa Oligomannosidic Glycoproteins of Rat Brain Are Signal Regulatory Proteins and Include the SHP Substrate-1 for Tyrosine Phosphatases" @default.
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- W2009764534 doi "https://doi.org/10.1046/j.1471-4159.1999.721688.x" @default.
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