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http://purl.uniprot.org/citations/6228551http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6228551http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6228551http://www.w3.org/2000/01/rdf-schema#comment"Lysosomal enzymes of the slime mold Dictyostelium discoideum contain mannose 6-phosphate and bind with high affinity to the phosphomannosyl receptor of human fibroblasts. In this study, we have partially characterized the Asn-linked oligosaccharide units present on these enzymes. [3H]Mannose-labeled alpha-D-mannosidase, beta-D-glucosidase, and beta-D-N-acetylglucosaminidase were purified from the spent growth medium of strain AX3 and glycopeptides were prepared by pronase digestion. Approximately 75% of the glycopeptides contained sulfate residues. These could be removed by solvolysis without degrading the underlying oligosaccharide. Following solvolysis (but not before), the oligosaccharides could be released by endo-beta-N-acetylglucosaminidase H, indicating the presence of high mannose-type units. Greater than 85% of the oligosaccharides contained one or two mannose 6-phosphate residues in the form of an unusual acid-stable phosphodiester. About 3% of the oligosaccharides contained phosphomonoesters and only 6% were neutral species. The major neutral oligosaccharide eluted in the position of Man9GlcNAc when analyzed by high performance liquid chromatography whereas the minor species appeared to be 1-2 residues larger. Acetolysis of the major phosphorylated fractions revealed that molecules with a single mannose 6-phosphate contained the phosphomannosyl residue on the branch linked alpha 1,6 to the beta-linked mannose whereas molecules with two phosphomannosyl residues had the residues on this branch as well as the branch linked alpha 1,3 to the beta-linked mannose. The mechanism of mannose phosphorylation in the slime mold must differ from that of mammalian cells since the phosphomannosyl residues are present as acid-resistant phosphodiesters rather than acid-labile phosphodiesters."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)43745-8"xsd:string
http://purl.uniprot.org/citations/6228551http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)43745-8"xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Freeze H.H."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Freeze H.H."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Kornfeld S."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Kornfeld S."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Miller A.L."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Miller A.L."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Yeh R."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/author"Yeh R."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/date"1983"xsd:gYear
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/date"1983"xsd:gYear
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/pages"14874-14879"xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/pages"14874-14879"xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/title"Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/title"Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester."xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/volume"258"xsd:string
http://purl.uniprot.org/citations/6228551http://purl.uniprot.org/core/volume"258"xsd:string
http://purl.uniprot.org/citations/6228551http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6228551
http://purl.uniprot.org/citations/6228551http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6228551
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