Abd El Wahed, Ahmed

[["dc.bibliographiccitation.firstpage","761"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","767"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Hasilik, A."],["dc.contributor.author","Waheed, A."],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:43Z"],["dc.date.available","2019-07-10T08:12:43Z"],["dc.date.issued","1981"],["dc.description.abstract","Summary: Recent finding of a-N-ocetylglucosamine( I)phospho(6)mannose diesters in lysosomal enzymes suggested that formation of monnose 6-phosphate residues involves transfer of N-acetylglucosamine l- hos hote to mannose. Using dephosphorylated R-hexosaminidase as acceptor and F t3-3 “I P UDP-N-acetylglucosamine OS donor for the phosphate group, phosphorylation of R-hexosaminidose by microsomes from rot liver, humon placenta and human skin fibroblosts wos achieved. The reaction was not affected by tunicomycin. Acid hydrolysis released monnose 6-[32P] phosphate from the phosphorylated l3-hexosaminidase. Our results suggest that lysosomal enzymes are phosphorylated by tronsfer of N-acetylglucosamine l-phosphate from UDP-N-ocetylglucosamine. The transferose activity wos deficient in fibroblasts from patients affected with l-cell disease. This deficiency is proposed to be the primary enzyme defect in I-ccl I disease."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3425"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61014"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Academic Press"],["dc.relation.issn","0006-291X"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","Enzymatic phosphorylation; lysosomal enzymes"],["dc.subject.ddc","610"],["dc.title","Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in I-cell fibroblasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7074"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","7078"],["dc.bibliographiccitation.volume","77"],["dc.contributor.author","Hasilik, A."],["dc.contributor.author","Klein, U."],["dc.contributor.author","Strecker, G."],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Abd El Wahed, Ahmed"],["dc.date.accessioned","2019-07-10T08:12:41Z"],["dc.date.available","2019-07-10T08:12:41Z"],["dc.date.issued","1980"],["dc.description.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."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3282"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61005"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","NAS"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","identification; α-N-acetylglucosamine (1) phospho(6)mannose; diester groups"],["dc.subject.ddc","610"],["dc.title","Phosphorylated oligosaccharides in lysosomal enzymes: identification of α-N-acetylglucosamine (1) phospho(6)mannose diester groups"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]