Phosphorylated oligosaccharides in lysosomal enzymes: identification of α-N-acetylglucosamine (1) phospho(6)mannose diester groups
1980 | journal article. A publication with affiliation to the University of Göttingen.
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Phosphorylated oligosaccharides in lysosomal enzymes: identification of α-N-acetylglucosamine (1) phospho(6)mannose diester groups
Hasilik, A.; Klein, U.; Strecker, G.; Figura, K. von & Abd El Wahed, A. (1980)
Proceedings of the National Academy of Sciences of the United States of America, 77(12) pp. 7074-7078.
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Details
- Authors
- Hasilik, A.; Klein, U.; Strecker, G.; Figura, Kurt von; Abd El Wahed, Ahmed
- Abstract
- In human fibroblasts, the recognition of lysosomal enzymes by cell surface receptors is mediated by mannose 6-phosphate residues located on oligosaccharides that can be cleaved by endo-β-N-acetylglucosaminidase H. About half of these oligosaccharides, as isolated from β-hexosaminidase and cathepsin D secreted by human skin fibroblasts, are anionic. Most of these are resistant to alkaline phosphatase. The resistance is due to α-N-acetylglucosamine residues linked to mannose 6phosphate by a phosphodiester bond. The major phosphorylated oligosaccharides contain one and two and possibly three phosphate groups blocked by N-acetylglucosamine. Besides the blocked phosphate groups these oligosaccharides contain a common inner core consisting of Manα1,6- (Manαl,3)Manαl,6(Manαl,3)ManβαGlcNAc and either one or two αl,2-linked mannose residues.
- Issue Date
- 1980
- Publisher
- NAS
- Journal
- Proceedings of the National Academy of Sciences of the United States of America
- File Format
- application/pdf
- Language
- English