PubMed:3094936 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":26,"end":47},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":61,"end":72},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":196,"end":217},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":673,"end":684},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1261,"end":1282},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1261,"end":1272},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1416,"end":1437},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1416,"end":1427},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G19059PI"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G34992DF"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1394,"end":1403},"obj":"http://purl.obolibrary.org/obo/MAT_0000189"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":91,"end":319},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":320,"end":395},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":396,"end":615},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":616,"end":694},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":695,"end":859},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":860,"end":928},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":929,"end":1073},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1074,"end":1209},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1210,"end":1438},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":395},"obj":"Sentence"},{"id":"T4","span":{"begin":396,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":694},"obj":"Sentence"},{"id":"T6","span":{"begin":695,"end":859},"obj":"Sentence"},{"id":"T7","span":{"begin":860,"end":928},"obj":"Sentence"},{"id":"T8","span":{"begin":929,"end":1073},"obj":"Sentence"},{"id":"T9","span":{"begin":1074,"end":1209},"obj":"Sentence"},{"id":"T10","span":{"begin":1210,"end":1438},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":26,"end":47},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T2","span":{"begin":61,"end":72},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T3","span":{"begin":196,"end":217},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T4","span":{"begin":673,"end":684},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T5","span":{"begin":1261,"end":1282},"obj":"https://glytoucan.org/Structures/Glycans/G19059PI"},{"id":"T6","span":{"begin":1261,"end":1272},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T7","span":{"begin":1416,"end":1437},"obj":"https://glytoucan.org/Structures/Glycans/G34992DF"},{"id":"T8","span":{"begin":1416,"end":1427},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":61,"end":72},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":673,"end":684},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T3","span":{"begin":1261,"end":1282},"obj":"http://www.glycoepitope.jp/epitopes/EP0082"},{"id":"T4","span":{"begin":1261,"end":1272},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T5","span":{"begin":1416,"end":1437},"obj":"http://www.glycoepitope.jp/epitopes/EP0083"},{"id":"T6","span":{"begin":1416,"end":1427},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":61,"end":72},"obj":"Glycan"},{"id":"T2","span":{"begin":219,"end":225},"obj":"Glycan"},{"id":"T3","span":{"begin":241,"end":247},"obj":"Glycan"},{"id":"T4","span":{"begin":358,"end":364},"obj":"Glycan"},{"id":"T5","span":{"begin":520,"end":526},"obj":"Glycan"},{"id":"T6","span":{"begin":580,"end":586},"obj":"Glycan"},{"id":"T7","span":{"begin":673,"end":684},"obj":"Glycan"},{"id":"T8","span":{"begin":751,"end":757},"obj":"Glycan"},{"id":"T9","span":{"begin":1137,"end":1143},"obj":"Glycan"},{"id":"T10","span":{"begin":1202,"end":1208},"obj":"Glycan"},{"id":"T11","span":{"begin":1261,"end":1282},"obj":"Glycan"},{"id":"T12","span":{"begin":1416,"end":1437},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A13","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A14","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A15","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A16","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A17","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A18","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A19","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A20","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A21","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A22","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G19059PI"},{"id":"A23","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G19059PI"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G34992DF"},{"id":"A24","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G34992DF"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":120,"end":123},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0010865"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":1226,"end":1237},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0002724"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0003079"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":61,"end":72},"obj":"Glycan"},{"id":"T2","span":{"begin":219,"end":225},"obj":"Glycan"},{"id":"T3","span":{"begin":241,"end":247},"obj":"Glycan"},{"id":"T4","span":{"begin":358,"end":364},"obj":"Glycan"},{"id":"T5","span":{"begin":520,"end":526},"obj":"Glycan"},{"id":"T6","span":{"begin":580,"end":586},"obj":"Glycan"},{"id":"T7","span":{"begin":673,"end":684},"obj":"Glycan"},{"id":"T8","span":{"begin":751,"end":757},"obj":"Glycan"},{"id":"T9","span":{"begin":1137,"end":1143},"obj":"Glycan"},{"id":"T10","span":{"begin":1202,"end":1208},"obj":"Glycan"},{"id":"T11","span":{"begin":1261,"end":1282},"obj":"Glycan"},{"id":"T12","span":{"begin":1416,"end":1437},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A13","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A14","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A15","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A16","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A17","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A18","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A19","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A20","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A21","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A22","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G19059PI"},{"id":"A23","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G19059PI"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G34992DF"},{"id":"A24","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G34992DF"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":1394,"end":1403},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":319},"obj":"Sentence"},{"id":"T3","span":{"begin":320,"end":395},"obj":"Sentence"},{"id":"T4","span":{"begin":396,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":694},"obj":"Sentence"},{"id":"T6","span":{"begin":695,"end":859},"obj":"Sentence"},{"id":"T7","span":{"begin":860,"end":928},"obj":"Sentence"},{"id":"T8","span":{"begin":929,"end":1073},"obj":"Sentence"},{"id":"T9","span":{"begin":1074,"end":1209},"obj":"Sentence"},{"id":"T10","span":{"begin":1210,"end":1438},"obj":"Sentence"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":61,"end":72},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":673,"end":684},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1261,"end":1282},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1416,"end":1437},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0082"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0083"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":1226,"end":1237},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0003079"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":1210,"end":1220},"obj":"Body_part"},{"id":"T2","span":{"begin":1372,"end":1382},"obj":"Body_part"},{"id":"T3","span":{"begin":1394,"end":1403},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:67438"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:67438"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:71500"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":1394,"end":1403},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000189"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":61,"end":72},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":673,"end":684},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1261,"end":1282},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1416,"end":1437},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0082"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0083"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1394,"end":1403},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1394,"end":1403},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000189"}],"text":"The effect of penultimate N-acetylgalactosamine 4-sulfate on chondroitin chain elongation.\nPrevious work has shown that odd-numbered oligosaccharides containing nonreducing terminal, non-sulfated N-acetylgalactosamine (GalNAc) or 6-sulfated GalNAc are excellent acceptors for enzymic addition of glucuronic acid (GlcA). However, the presence of a 4-sulfated GalNAc group blocks further addition. We have now used even-numbered oligosaccharides (a mixture of 4-sulfated, 6-sulfated, and non-sulfated) as acceptors of [3H]GalNAc to investigate the effect of sulfate residues on the GalNAc in the penultimate position. 3H-Labeled oligosaccharides were partially degraded with chondroitin AC lyase. The labeled trisaccharides, consisting of the added [3H]GalNAc and the nonreducing terminal disaccharides of the oligosaccharide acceptors, were then characterized. Both non-sulfated and mono-sulfated 3H-trisaccharides were observed. However, the 3H-trisaccharides were shown by chromatography with prepared standards to be non-sulfated or to be sulfated only at the 6-position. Thus the oligosaccharides containing a 4-sulfated, penultimate GalNAc at the nonreducing end did not serve as acceptors for [3H]GalNAc. Microsomes from mastocytoma cells, which make only chondroitin 4-sulfate, exhibited the same substrate specificity for exogenous oligosaccharide acceptors as did microsomes from chick cartilage which makes chondroitin 6-sulfate."}