PubMed:10024660 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":126},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":127,"end":369},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":370,"end":474},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":475,"end":658},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":659,"end":856},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":857,"end":1042},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":126},"obj":"Sentence"},{"id":"T2","span":{"begin":127,"end":369},"obj":"Sentence"},{"id":"T3","span":{"begin":370,"end":474},"obj":"Sentence"},{"id":"T4","span":{"begin":475,"end":658},"obj":"Sentence"},{"id":"T5","span":{"begin":659,"end":856},"obj":"Sentence"},{"id":"T6","span":{"begin":857,"end":1042},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":126},"obj":"Sentence"},{"id":"T2","span":{"begin":127,"end":369},"obj":"Sentence"},{"id":"T3","span":{"begin":370,"end":474},"obj":"Sentence"},{"id":"T4","span":{"begin":475,"end":658},"obj":"Sentence"},{"id":"T5","span":{"begin":659,"end":856},"obj":"Sentence"},{"id":"T6","span":{"begin":857,"end":1042},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":44,"end":60},"obj":"FMAID:82742"},{"id":"_T2","span":{"begin":44,"end":60},"obj":"FMAID:196731"},{"id":"_T3","span":{"begin":64,"end":68},"obj":"FMAID:167334"},{"id":"_T4","span":{"begin":114,"end":120},"obj":"FMAID:97486"},{"id":"_T5","span":{"begin":114,"end":120},"obj":"FMAID:9601"},{"id":"_T6","span":{"begin":121,"end":125},"obj":"FMAID:165676"},{"id":"_T7","span":{"begin":178,"end":182},"obj":"FMAID:167334"},{"id":"_T8","span":{"begin":228,"end":232},"obj":"FMAID:165676"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":207,"end":211},"obj":"http://www.uniprot.org/uniprot/P19835"},{"id":"T2","span":{"begin":722,"end":726},"obj":"http://www.uniprot.org/uniprot/P19835"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":207,"end":211},"obj":"http://www.uniprot.org/uniprot/Q64285"},{"id":"T2","span":{"begin":722,"end":726},"obj":"http://www.uniprot.org/uniprot/Q64285"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":308,"end":313},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62990"},{"id":"T2","span":{"begin":427,"end":432},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62951"},{"id":"T3","span":{"begin":912,"end":922},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/242975"},{"id":"T4","span":{"begin":944,"end":954},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/242975"},{"id":"T5","span":{"begin":979,"end":989},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/242975"},{"id":"T6","span":{"begin":1022,"end":1032},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/242975"},{"id":"T7","span":{"begin":1033,"end":1041},"obj":"http://purl.bioontology.org/ontology/STY/T071"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

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The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":277,"end":286},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T2","span":{"begin":344,"end":350},"obj":"http://purl.obolibrary.org/obo/GO_0060361"},{"id":"T3","span":{"begin":461,"end":473},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T4","span":{"begin":924,"end":935},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T5","span":{"begin":1010,"end":1021},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T6","span":{"begin":479,"end":487},"obj":"http://purl.obolibrary.org/obo/GO_0015297"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":64,"end":68},"obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"T2","span":{"begin":178,"end":182},"obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"T3","span":{"begin":114,"end":120},"obj":"http://purl.obolibrary.org/obo/UBERON_0000310"},{"id":"T4","span":{"begin":121,"end":125},"obj":"http://purl.obolibrary.org/obo/UBERON_0001913"},{"id":"T5","span":{"begin":228,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0001913"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":108,"end":113},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":222,"end":227},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":351,"end":368},"obj":"http://edamontology.org/topic_0134"},{"id":"T4","span":{"begin":351,"end":368},"obj":"http://edamontology.org/topic_3520"},{"id":"T5","span":{"begin":763,"end":770},"obj":"http://edamontology.org/topic_3678"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://edamontology.org/data_0883"},{"id":"T2","span":{"begin":140,"end":150},"obj":"http://edamontology.org/data_0883"},{"id":"T3","span":{"begin":292,"end":298},"obj":"http://edamontology.org/data_2082"},{"id":"T4","span":{"begin":351,"end":368},"obj":"http://edamontology.org/data_3147"},{"id":"T5","span":{"begin":351,"end":368},"obj":"http://edamontology.org/data_2536"},{"id":"T6","span":{"begin":384,"end":394},"obj":"http://edamontology.org/data_0883"},{"id":"T7","span":{"begin":427,"end":432},"obj":"http://edamontology.org/data_0968"},{"id":"T8","span":{"begin":528,"end":537},"obj":"http://edamontology.org/operation_2423"},{"id":"T9","span":{"begin":553,"end":575},"obj":"http://edamontology.org/operation_3214"},{"id":"T10","span":{"begin":558,"end":575},"obj":"http://edamontology.org/operation_3214"},{"id":"T11","span":{"begin":567,"end":575},"obj":"http://edamontology.org/operation_2945"},{"id":"T12","span":{"begin":647,"end":657},"obj":"http://edamontology.org/data_0883"},{"id":"T13","span":{"begin":663,"end":677},"obj":"http://edamontology.org/data_0844"},{"id":"T14","span":{"begin":871,"end":881},"obj":"http://edamontology.org/data_0883"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":154,"end":164},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":594,"end":604},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T3","span":{"begin":374,"end":383},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T4","span":{"begin":861,"end":870},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":64,"end":68},"obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":178,"end":182},"obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":114,"end":120},"obj":"http://purl.obolibrary.org/obo/UBERON_0000310"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":121,"end":125},"obj":"http://purl.obolibrary.org/obo/UBERON_0001913"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":228,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0001913"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":108,"end":113},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":222,"end":227},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":64,"end":68},"obj":"Body_part"},{"id":"T2","span":{"begin":114,"end":120},"obj":"Body_part"},{"id":"T3","span":{"begin":121,"end":125},"obj":"Body_part"},{"id":"T4","span":{"begin":178,"end":182},"obj":"Body_part"},{"id":"T5","span":{"begin":228,"end":232},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000310"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001913"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001970"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001913"}],"text":"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.\nThe detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities."}