PubMed:19240272 JSONTXT

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    Glycan-Motif

    {"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1133,"end":1145},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1603,"end":1610},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos6-Glycan-Motif-Image

    {"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1133,"end":1145},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1603,"end":1610},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    PMID_GLOBAL

    {"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":580,"end":582},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":589,"end":591},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":592,"end":594},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0006861"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"0006861"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"0006861"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":85,"end":212},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":213,"end":343},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":344,"end":604},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":605,"end":731},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":732,"end":1002},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1003,"end":1154},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1155,"end":1300},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1301,"end":1485},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1486,"end":1671},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1672,"end":1987},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"T2","span":{"begin":85,"end":212},"obj":"Sentence"},{"id":"T3","span":{"begin":213,"end":343},"obj":"Sentence"},{"id":"T4","span":{"begin":344,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":731},"obj":"Sentence"},{"id":"T6","span":{"begin":732,"end":1002},"obj":"Sentence"},{"id":"T7","span":{"begin":1003,"end":1154},"obj":"Sentence"},{"id":"T8","span":{"begin":1155,"end":1300},"obj":"Sentence"},{"id":"T9","span":{"begin":1301,"end":1485},"obj":"Sentence"},{"id":"T10","span":{"begin":1486,"end":1671},"obj":"Sentence"},{"id":"T11","span":{"begin":1672,"end":1987},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"T2","span":{"begin":85,"end":212},"obj":"Sentence"},{"id":"T3","span":{"begin":213,"end":343},"obj":"Sentence"},{"id":"T4","span":{"begin":344,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":731},"obj":"Sentence"},{"id":"T6","span":{"begin":732,"end":1002},"obj":"Sentence"},{"id":"T7","span":{"begin":1003,"end":1154},"obj":"Sentence"},{"id":"T8","span":{"begin":1155,"end":1300},"obj":"Sentence"},{"id":"T9","span":{"begin":1301,"end":1485},"obj":"Sentence"},{"id":"T10","span":{"begin":1486,"end":1671},"obj":"Sentence"},{"id":"T11","span":{"begin":1672,"end":1987},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos6-Glycan-Motif-Structure

    {"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1133,"end":1145},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1603,"end":1610},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    Glycosmos6-MAT

    {"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T2","span":{"begin":71,"end":74},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T3","span":{"begin":311,"end":314},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T4","span":{"begin":468,"end":471},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T5","span":{"begin":539,"end":542},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T6","span":{"begin":1027,"end":1030},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T7","span":{"begin":1306,"end":1309},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlycoBiology-FMA

    {"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":53,"end":66},"obj":"FMAID:167256"},{"id":"_T2","span":{"begin":53,"end":66},"obj":"FMAID:62925"},{"id":"_T3","span":{"begin":80,"end":83},"obj":"FMAID:167179"},{"id":"_T4","span":{"begin":156,"end":169},"obj":"FMAID:167256"},{"id":"_T5","span":{"begin":156,"end":169},"obj":"FMAID:62925"},{"id":"_T6","span":{"begin":321,"end":334},"obj":"FMAID:62925"},{"id":"_T7","span":{"begin":321,"end":334},"obj":"FMAID:167256"},{"id":"_T8","span":{"begin":339,"end":342},"obj":"FMAID:167179"},{"id":"_T9","span":{"begin":484,"end":497},"obj":"FMAID:62925"},{"id":"_T10","span":{"begin":484,"end":497},"obj":"FMAID:167256"},{"id":"_T11","span":{"begin":548,"end":551},"obj":"FMAID:167179"},{"id":"_T12","span":{"begin":609,"end":622},"obj":"FMAID:167256"},{"id":"_T13","span":{"begin":609,"end":622},"obj":"FMAID:62925"},{"id":"_T14","span":{"begin":763,"end":779},"obj":"FMAID:82742"},{"id":"_T15","span":{"begin":763,"end":779},"obj":"FMAID:196731"},{"id":"_T16","span":{"begin":937,"end":945},"obj":"FMAID:226027"},{"id":"_T17","span":{"begin":937,"end":945},"obj":"FMAID:226028"},{"id":"_T18","span":{"begin":1037,"end":1050},"obj":"FMAID:167256"},{"id":"_T19","span":{"begin":1037,"end":1050},"obj":"FMAID:62925"},{"id":"_T20","span":{"begin":1081,"end":1094},"obj":"FMAID:62925"},{"id":"_T21","span":{"begin":1081,"end":1094},"obj":"FMAID:167256"},{"id":"_T22","span":{"begin":1187,"end":1202},"obj":"FMAID:196731"},{"id":"_T23","span":{"begin":1187,"end":1202},"obj":"FMAID:82742"},{"id":"_T24","span":{"begin":1216,"end":1232},"obj":"FMAID:196731"},{"id":"_T25","span":{"begin":1216,"end":1232},"obj":"FMAID:82742"},{"id":"_T26","span":{"begin":1286,"end":1299},"obj":"FMAID:62925"},{"id":"_T27","span":{"begin":1286,"end":1299},"obj":"FMAID:167256"},{"id":"_T28","span":{"begin":1315,"end":1318},"obj":"FMAID:167179"},{"id":"_T29","span":{"begin":1403,"end":1406},"obj":"FMAID:167179"},{"id":"_T30","span":{"begin":1521,"end":1537},"obj":"FMAID:82742"},{"id":"_T31","span":{"begin":1521,"end":1537},"obj":"FMAID:196731"},{"id":"_T32","span":{"begin":1603,"end":1610},"obj":"FMAID:196796"},{"id":"_T33","span":{"begin":1603,"end":1610},"obj":"FMAID:82801"},{"id":"_T34","span":{"begin":1616,"end":1632},"obj":"FMAID:82742"},{"id":"_T35","span":{"begin":1616,"end":1632},"obj":"FMAID:196731"},{"id":"_T36","span":{"begin":1667,"end":1670},"obj":"FMAID:167179"},{"id":"_T37","span":{"begin":1725,"end":1738},"obj":"FMAID:167256"},{"id":"_T38","span":{"begin":1725,"end":1738},"obj":"FMAID:62925"},{"id":"_T39","span":{"begin":1748,"end":1751},"obj":"FMAID:167179"},{"id":"_T40","span":{"begin":1973,"end":1986},"obj":"FMAID:62925"},{"id":"_T41","span":{"begin":1973,"end":1986},"obj":"FMAID:167256"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    uniprot-human

    {"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":580,"end":582},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T2","span":{"begin":589,"end":591},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T3","span":{"begin":592,"end":594},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T4","span":{"begin":1351,"end":1357},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T5","span":{"begin":1366,"end":1372},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T6","span":{"begin":1428,"end":1434},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T7","span":{"begin":1440,"end":1446},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T8","span":{"begin":1455,"end":1461},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T9","span":{"begin":1781,"end":1787},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T10","span":{"begin":1796,"end":1802},"obj":"http://www.uniprot.org/uniprot/Q92988"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    uniprot-mouse

    {"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":580,"end":582},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T2","span":{"begin":589,"end":591},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T3","span":{"begin":592,"end":594},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlycoBiology-NCBITAXON

    {"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":176,"end":181},"obj":"http://purl.bioontology.org/ontology/STY/T012"},{"id":"T2","span":{"begin":185,"end":192},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T3","span":{"begin":747,"end":752},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1310384"},{"id":"T4","span":{"begin":747,"end":752},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/85284"},{"id":"T5","span":{"begin":753,"end":762},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/293542"},{"id":"T6","span":{"begin":1351,"end":1355},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T7","span":{"begin":1351,"end":1355},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T8","span":{"begin":1366,"end":1370},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T9","span":{"begin":1366,"end":1370},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T10","span":{"begin":1428,"end":1432},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T11","span":{"begin":1428,"end":1432},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T12","span":{"begin":1440,"end":1444},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T13","span":{"begin":1440,"end":1444},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T14","span":{"begin":1455,"end":1459},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T15","span":{"begin":1455,"end":1459},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T16","span":{"begin":1498,"end":1507},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/293542"},{"id":"T17","span":{"begin":1781,"end":1785},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T18","span":{"begin":1781,"end":1785},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T19","span":{"begin":1796,"end":1800},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T20","span":{"begin":1796,"end":1800},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T21","span":{"begin":1860,"end":1863},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":882,"end":893},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T2","span":{"begin":1062,"end":1073},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":1574,"end":1586},"obj":"http://purl.obolibrary.org/obo/GO_0036065"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":824,"end":828},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T2","span":{"begin":1569,"end":1573},"obj":"http://purl.obolibrary.org/obo/GO_0019013"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    UBERON-AE

    {"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T2","span":{"begin":71,"end":74},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T3","span":{"begin":311,"end":314},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T4","span":{"begin":468,"end":471},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T5","span":{"begin":539,"end":542},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T6","span":{"begin":1027,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T7","span":{"begin":1306,"end":1309},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"T8","span":{"begin":71,"end":79},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"T9","span":{"begin":539,"end":547},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"T10","span":{"begin":1306,"end":1314},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"T11","span":{"begin":75,"end":79},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"},{"id":"T12","span":{"begin":543,"end":547},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"},{"id":"T13","span":{"begin":1310,"end":1314},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    NGLY1-deficiency

    {"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":802,"end":808},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1253,"end":1259},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1553,"end":1559},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlycoBiology-MAT

    {"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T2","span":{"begin":71,"end":74},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T3","span":{"begin":311,"end":314},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T4","span":{"begin":468,"end":471},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T5","span":{"begin":539,"end":542},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T6","span":{"begin":1027,"end":1030},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T7","span":{"begin":1306,"end":1309},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlycoBiology-Motifs

    {"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":23,"end":32},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":274,"end":283},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T3","span":{"begin":408,"end":417},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T4","span":{"begin":450,"end":459},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T5","span":{"begin":666,"end":675},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T6","span":{"begin":1701,"end":1710},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T7","span":{"begin":982,"end":990},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T8","span":{"begin":1598,"end":1610},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyTouCan-IUPAC

    {"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":130,"end":133},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T2","span":{"begin":245,"end":248},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T3","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T4","span":{"begin":704,"end":707},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T5","span":{"begin":1334,"end":1337},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T6","span":{"begin":1411,"end":1414},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T7","span":{"begin":1764,"end":1767},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T8","span":{"begin":1837,"end":1840},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T9","span":{"begin":1870,"end":1873},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T10","span":{"begin":130,"end":133},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T11","span":{"begin":245,"end":248},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T12","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T13","span":{"begin":704,"end":707},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T14","span":{"begin":1334,"end":1337},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T15","span":{"begin":1411,"end":1414},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T16","span":{"begin":1764,"end":1767},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T17","span":{"begin":1837,"end":1840},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T18","span":{"begin":1870,"end":1873},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T19","span":{"begin":130,"end":133},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T20","span":{"begin":245,"end":248},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T21","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T22","span":{"begin":704,"end":707},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T23","span":{"begin":1334,"end":1337},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T24","span":{"begin":1411,"end":1414},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T25","span":{"begin":1764,"end":1767},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T26","span":{"begin":1837,"end":1840},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T27","span":{"begin":1870,"end":1873},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T28","span":{"begin":130,"end":133},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T29","span":{"begin":245,"end":248},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T30","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T31","span":{"begin":704,"end":707},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T32","span":{"begin":1334,"end":1337},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T33","span":{"begin":1411,"end":1414},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T34","span":{"begin":1764,"end":1767},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T35","span":{"begin":1837,"end":1840},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T36","span":{"begin":1870,"end":1873},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T37","span":{"begin":130,"end":133},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T38","span":{"begin":245,"end":248},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T39","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T40","span":{"begin":704,"end":707},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T41","span":{"begin":1334,"end":1337},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T42","span":{"begin":1411,"end":1414},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T43","span":{"begin":1764,"end":1767},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T44","span":{"begin":1837,"end":1840},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T45","span":{"begin":1870,"end":1873},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"Gly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http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T1349","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T1350","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T1351","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T1352","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T1353","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T1354","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T1355","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T1356","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T1357","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T1358","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T1359","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T1360","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T1361","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T1362","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T1363","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T1364","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T1365","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T1366","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T1367","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T1368","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T1369","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T1370","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T1371","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T1372","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T1373","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T1374","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T1375","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T1376","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T1377","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T1378","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T1379","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T1380","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T1381","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T1382","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T1383","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T1384","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T1385","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T1386","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T1387","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T1388","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T1389","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T1390","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T1391","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T1392","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T1393","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T1394","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T1395","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T1396","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T1397","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T1398","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T1399","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T1400","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T1401","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T1402","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T1403","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T1404","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T1405","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T1406","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T1407","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T1408","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T1409","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T1410","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T1411","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T1412","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T1413","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T1414","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T1415","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T1416","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T1417","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T1418","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T1419","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T1420","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T1421","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T1422","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T1423","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T1424","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T1425","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T1426","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T1427","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T1428","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T1429","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T1430","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T1431","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T1432","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T1433","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T1434","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T1435","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T1436","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T1437","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T1438","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T1439","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T1440","span":{"begin":802,"end":808},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T1441","span":{"begin":1253,"end":1259},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T1442","span":{"begin":1553,"end":1559},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T1443","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T1444","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T1445","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T1446","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T1447","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T1448","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T1449","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T1450","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T1451","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T1452","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T1453","span":{"begin":1860,"end":1863},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    performance-test

    {"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":43,"end":46},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":71,"end":74},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":311,"end":314},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":468,"end":471},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":539,"end":542},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":1027,"end":1030},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":1306,"end":1309},"obj":"http://purl.obolibrary.org/obo/UBERON_0007379"},{"id":"PD-UBERON-AE-B_T8","span":{"begin":71,"end":79},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"PD-UBERON-AE-B_T9","span":{"begin":539,"end":547},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"PD-UBERON-AE-B_T10","span":{"begin":1306,"end":1314},"obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"PD-UBERON-AE-B_T11","span":{"begin":75,"end":79},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"},{"id":"PD-UBERON-AE-B_T12","span":{"begin":543,"end":547},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"},{"id":"PD-UBERON-AE-B_T13","span":{"begin":1310,"end":1314},"obj":"http://purl.obolibrary.org/obo/UBERON_2000084"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos15-Glycan

    {"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1147,"end":1152},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    Glycan-GlyCosmos

    {"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1147,"end":1152},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos15-Taxon

    {"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":38,"end":42},"obj":"Organism"},{"id":"T2","span":{"begin":463,"end":467},"obj":"Organism"},{"id":"T3","span":{"begin":534,"end":538},"obj":"Organism"},{"id":"T4","span":{"begin":1662,"end":1666},"obj":"Organism"},{"id":"T5","span":{"begin":1743,"end":1747},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"8910"},{"id":"A2","pred":"db_id","subj":"T2","obj":"8910"},{"id":"A3","pred":"db_id","subj":"T3","obj":"8910"},{"id":"A4","pred":"db_id","subj":"T4","obj":"8910"},{"id":"A5","pred":"db_id","subj":"T5","obj":"8910"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos15-Sentences

    {"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"T2","span":{"begin":85,"end":212},"obj":"Sentence"},{"id":"T3","span":{"begin":213,"end":343},"obj":"Sentence"},{"id":"T4","span":{"begin":344,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":731},"obj":"Sentence"},{"id":"T6","span":{"begin":732,"end":1002},"obj":"Sentence"},{"id":"T7","span":{"begin":1003,"end":1154},"obj":"Sentence"},{"id":"T8","span":{"begin":1155,"end":1300},"obj":"Sentence"},{"id":"T9","span":{"begin":1301,"end":1485},"obj":"Sentence"},{"id":"T10","span":{"begin":1486,"end":1671},"obj":"Sentence"},{"id":"T11","span":{"begin":1672,"end":1987},"obj":"Sentence"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos15-UBERON

    {"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":43,"end":52},"obj":"Body_part"},{"id":"T2","span":{"begin":71,"end":79},"obj":"Body_part"},{"id":"T3","span":{"begin":311,"end":320},"obj":"Body_part"},{"id":"T4","span":{"begin":468,"end":477},"obj":"Body_part"},{"id":"T5","span":{"begin":539,"end":547},"obj":"Body_part"},{"id":"T6","span":{"begin":1027,"end":1036},"obj":"Body_part"},{"id":"T7","span":{"begin":1306,"end":1314},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    GlyCosmos15-MAT

    {"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"Body_part"},{"id":"T2","span":{"begin":71,"end":74},"obj":"Body_part"},{"id":"T3","span":{"begin":311,"end":314},"obj":"Body_part"},{"id":"T4","span":{"begin":468,"end":471},"obj":"Body_part"},{"id":"T5","span":{"begin":539,"end":542},"obj":"Body_part"},{"id":"T6","span":{"begin":1027,"end":1030},"obj":"Body_part"},{"id":"T7","span":{"begin":1306,"end":1309},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000213"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    NCBITAXON

    {"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":38,"end":42},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":463,"end":467},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":534,"end":538},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1301,"end":1305},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1662,"end":1666},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1743,"end":1747},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"8910"},{"id":"A2","pred":"db_id","subj":"T2","obj":"8910"},{"id":"A3","pred":"db_id","subj":"T3","obj":"8910"},{"id":"A4","pred":"db_id","subj":"T4","obj":"8910"},{"id":"A5","pred":"db_id","subj":"T5","obj":"8910"},{"id":"A6","pred":"db_id","subj":"T6","obj":"8910"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    Anatomy-MAT

    {"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":43,"end":46},"obj":"Body_part"},{"id":"T2","span":{"begin":71,"end":74},"obj":"Body_part"},{"id":"T3","span":{"begin":311,"end":314},"obj":"Body_part"},{"id":"T4","span":{"begin":468,"end":471},"obj":"Body_part"},{"id":"T5","span":{"begin":539,"end":542},"obj":"Body_part"},{"id":"T6","span":{"begin":1027,"end":1030},"obj":"Body_part"},{"id":"T7","span":{"begin":1306,"end":1309},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000213"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}

    Anatomy-UBERON

    {"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":43,"end":52},"obj":"Body_part"},{"id":"T2","span":{"begin":71,"end":79},"obj":"Body_part"},{"id":"T3","span":{"begin":311,"end":320},"obj":"Body_part"},{"id":"T4","span":{"begin":468,"end":477},"obj":"Body_part"},{"id":"T5","span":{"begin":539,"end":547},"obj":"Body_part"},{"id":"T6","span":{"begin":1027,"end":1036},"obj":"Body_part"},{"id":"T7","span":{"begin":1306,"end":1314},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0008944"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0007378"}],"text":"Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.\nWe previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins."}