PubMed:21484392 JSONTXT

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    GlyCosmos6-Glycan-Motif-Image

    {"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1109,"end":1128},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":47},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":48,"end":248},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":249,"end":421},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":422,"end":571},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":572,"end":714},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":715,"end":789},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":790,"end":848},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":849,"end":1004},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1005,"end":1129},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1130,"end":1292},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1293,"end":1343},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":47},"obj":"Sentence"},{"id":"T2","span":{"begin":48,"end":248},"obj":"Sentence"},{"id":"T3","span":{"begin":249,"end":421},"obj":"Sentence"},{"id":"T4","span":{"begin":422,"end":571},"obj":"Sentence"},{"id":"T5","span":{"begin":572,"end":714},"obj":"Sentence"},{"id":"T6","span":{"begin":715,"end":789},"obj":"Sentence"},{"id":"T7","span":{"begin":790,"end":848},"obj":"Sentence"},{"id":"T8","span":{"begin":849,"end":1004},"obj":"Sentence"},{"id":"T9","span":{"begin":1005,"end":1129},"obj":"Sentence"},{"id":"T10","span":{"begin":1130,"end":1292},"obj":"Sentence"},{"id":"T11","span":{"begin":1293,"end":1343},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    GlyCosmos6-Glycan-Motif-Structure

    {"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1109,"end":1128},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    Glycosmos6-MAT

    {"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":37,"end":40},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T2","span":{"begin":72,"end":75},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T3","span":{"begin":139,"end":142},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T4","span":{"begin":183,"end":186},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"},{"id":"T5","span":{"begin":668,"end":672},"obj":"http://purl.obolibrary.org/obo/MAT_0000213"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    NGLY1-deficiency

    {"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1109,"end":1128},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1276,"end":1282},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1184,"end":1190},"obj":"hgnc:17646"}],"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":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    Anatomy-MAT

    {"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":37,"end":40},"obj":"Body_part"},{"id":"T2","span":{"begin":72,"end":75},"obj":"Body_part"},{"id":"T3","span":{"begin":139,"end":142},"obj":"Body_part"},{"id":"T4","span":{"begin":183,"end":186},"obj":"Body_part"},{"id":"T5","span":{"begin":668,"end":672},"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"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}

    Anatomy-UBERON

    {"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"Body_part"},{"id":"T2","span":{"begin":72,"end":81},"obj":"Body_part"},{"id":"T3","span":{"begin":139,"end":148},"obj":"Body_part"},{"id":"T4","span":{"begin":183,"end":192},"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_0008944"},{"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"}],"text":"N-glycosylation of ovomucin from hen egg white.\nOvomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin."}