PubMed:15604092 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1025,"end":1034},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":1025,"end":1034},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":1072,"end":1091},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T4","span":{"begin":1193,"end":1200},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1025,"end":1034},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1072,"end":1091},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1193,"end":1200},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":147,"end":300},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":301,"end":434},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":435,"end":612},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":613,"end":930},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":931,"end":1044},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1045,"end":1147},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1148,"end":1246},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1247,"end":1313},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1314,"end":1611},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1612,"end":1859},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":434},"obj":"Sentence"},{"id":"T4","span":{"begin":435,"end":612},"obj":"Sentence"},{"id":"T5","span":{"begin":613,"end":930},"obj":"Sentence"},{"id":"T6","span":{"begin":931,"end":1044},"obj":"Sentence"},{"id":"T7","span":{"begin":1045,"end":1147},"obj":"Sentence"},{"id":"T8","span":{"begin":1148,"end":1246},"obj":"Sentence"},{"id":"T9","span":{"begin":1247,"end":1313},"obj":"Sentence"},{"id":"T10","span":{"begin":1314,"end":1611},"obj":"Sentence"},{"id":"T11","span":{"begin":1612,"end":1859},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":434},"obj":"Sentence"},{"id":"T4","span":{"begin":435,"end":612},"obj":"Sentence"},{"id":"T5","span":{"begin":613,"end":930},"obj":"Sentence"},{"id":"T6","span":{"begin":931,"end":1044},"obj":"Sentence"},{"id":"T7","span":{"begin":1045,"end":1147},"obj":"Sentence"},{"id":"T8","span":{"begin":1148,"end":1246},"obj":"Sentence"},{"id":"T9","span":{"begin":1247,"end":1313},"obj":"Sentence"},{"id":"T10","span":{"begin":1314,"end":1611},"obj":"Sentence"},{"id":"T11","span":{"begin":1612,"end":1859},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1025,"end":1034},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":1025,"end":1034},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":1072,"end":1091},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T4","span":{"begin":1193,"end":1200},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":68,"end":71},"obj":"http://www.uniprot.org/uniprot/Q05996"},{"id":"T2","span":{"begin":282,"end":285},"obj":"http://www.uniprot.org/uniprot/Q05996"},{"id":"T3","span":{"begin":528,"end":531},"obj":"http://www.uniprot.org/uniprot/Q05996"},{"id":"T4","span":{"begin":673,"end":676},"obj":"http://www.uniprot.org/uniprot/Q05996"},{"id":"T5","span":{"begin":1441,"end":1444},"obj":"http://www.uniprot.org/uniprot/Q05996"},{"id":"T6","span":{"begin":85,"end":87},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T7","span":{"begin":872,"end":874},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T8","span":{"begin":1247,"end":1249},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T9","span":{"begin":1250,"end":1252},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T10","span":{"begin":1608,"end":1610},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T11","span":{"begin":1771,"end":1773},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T12","span":{"begin":287,"end":290},"obj":"http://www.uniprot.org/uniprot/Q12836"},{"id":"T13","span":{"begin":389,"end":392},"obj":"http://www.uniprot.org/uniprot/Q12836"},{"id":"T14","span":{"begin":296,"end":299},"obj":"http://www.uniprot.org/uniprot/P21754"},{"id":"T15","span":{"begin":393,"end":396},"obj":"http://www.uniprot.org/uniprot/P21754"},{"id":"T16","span":{"begin":771,"end":789},"obj":"http://www.uniprot.org/uniprot/P16278"},{"id":"T17","span":{"begin":1366,"end":1384},"obj":"http://www.uniprot.org/uniprot/P16278"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":85,"end":87},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T2","span":{"begin":872,"end":874},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T3","span":{"begin":1247,"end":1249},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T4","span":{"begin":1250,"end":1252},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T5","span":{"begin":1608,"end":1610},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T6","span":{"begin":1771,"end":1773},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T7","span":{"begin":771,"end":789},"obj":"http://www.uniprot.org/uniprot/P23780"},{"id":"T8","span":{"begin":1366,"end":1384},"obj":"http://www.uniprot.org/uniprot/P23780"},{"id":"T9","span":{"begin":1542,"end":1545},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T10","span":{"begin":1699,"end":1702},"obj":"http://www.uniprot.org/uniprot/Q61024"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":643,"end":662},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/8004"},{"id":"T2","span":{"begin":771,"end":775},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":771,"end":775},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T4","span":{"begin":1366,"end":1370},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T5","span":{"begin":1366,"end":1370},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":360,"end":373},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":477,"end":490},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":1519,"end":1532},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T4","span":{"begin":1642,"end":1654},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":1136,"end":1146},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T6","span":{"begin":1162,"end":1168},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T7","span":{"begin":1344,"end":1353},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T8","span":{"begin":1428,"end":1437},"obj":"http://purl.obolibrary.org/obo/GO_0007586"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":121,"end":145},"obj":"http://purl.obolibrary.org/obo/GO_0035804"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":196,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0005576"},{"id":"T2","span":{"begin":196,"end":216},"obj":"http://purl.obolibrary.org/obo/GO_0031012"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":40,"end":54},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"T2","span":{"begin":121,"end":135},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"T3","span":{"begin":222,"end":236},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":454,"end":462},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":1304,"end":1312},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T3","span":{"begin":1188,"end":1200},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":40,"end":54},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":121,"end":135},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":222,"end":236},"obj":"http://purl.obolibrary.org/obo/UBERON_0000086"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":1450,"end":1456},"obj":"lectin"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":434},"obj":"Sentence"},{"id":"T4","span":{"begin":435,"end":612},"obj":"Sentence"},{"id":"T5","span":{"begin":613,"end":930},"obj":"Sentence"},{"id":"T6","span":{"begin":931,"end":1044},"obj":"Sentence"},{"id":"T7","span":{"begin":1045,"end":1147},"obj":"Sentence"},{"id":"T8","span":{"begin":1148,"end":1246},"obj":"Sentence"},{"id":"T9","span":{"begin":1247,"end":1313},"obj":"Sentence"},{"id":"T10","span":{"begin":1314,"end":1611},"obj":"Sentence"},{"id":"T11","span":{"begin":1612,"end":1859},"obj":"Sentence"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":40,"end":54},"obj":"Body_part"},{"id":"T4","span":{"begin":121,"end":135},"obj":"Body_part"},{"id":"T7","span":{"begin":161,"end":167},"obj":"Body_part"},{"id":"T8","span":{"begin":196,"end":216},"obj":"Body_part"},{"id":"T9","span":{"begin":222,"end":236},"obj":"Body_part"},{"id":"T12","span":{"begin":238,"end":240},"obj":"Body_part"},{"id":"T13","span":{"begin":338,"end":340},"obj":"Body_part"},{"id":"T14","span":{"begin":512,"end":514},"obj":"Body_part"},{"id":"T15","span":{"begin":547,"end":553},"obj":"Body_part"},{"id":"T16","span":{"begin":1393,"end":1395},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003125"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0003125"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000023"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/GO_0031012"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A10","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000086"},{"id":"A11","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0003125"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A13","pred":"uberon_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A14","pred":"uberon_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/GO_0035805"},{"id":"A15","pred":"uberon_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CL_0000023"},{"id":"A16","pred":"uberon_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/GO_0035805"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":161,"end":167},"obj":"Cell"},{"id":"T2","span":{"begin":547,"end":553},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000023"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000023"}],"text":"Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure.\nThe mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides."}