PubMed:12634322 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":71,"end":78},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":71,"end":78},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":118,"end":125},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T4","span":{"begin":118,"end":125},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T5","span":{"begin":194,"end":205},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T6","span":{"begin":771,"end":792},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T7","span":{"begin":919,"end":940},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T8","span":{"begin":1521,"end":1528},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T9","span":{"begin":1521,"end":1528},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":71,"end":78},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":118,"end":125},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":194,"end":205},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":771,"end":792},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":919,"end":940},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1521,"end":1528},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G54161DR"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00021MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G54161DR"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00021MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G54161DR"},{"id":"A9","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00021MO"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1432,"end":1593},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"T9","span":{"begin":1432,"end":1593},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"T9","span":{"begin":1432,"end":1593},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":71,"end":78},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":71,"end":78},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":118,"end":125},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T4","span":{"begin":118,"end":125},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T5","span":{"begin":194,"end":205},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T6","span":{"begin":771,"end":792},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T7","span":{"begin":919,"end":940},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T8","span":{"begin":1521,"end":1528},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T9","span":{"begin":1521,"end":1528},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":194,"end":205},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":225,"end":240},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":333,"end":339},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":358,"end":365},"obj":"http://purl.obolibrary.org/obo/MAT_0000226"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T20","span":{"begin":392,"end":403},"obj":"FMAID:196792"},{"id":"_T1","span":{"begin":0,"end":17},"obj":"FMAID:63011"},{"id":"_T2","span":{"begin":0,"end":17},"obj":"FMAID:167395"},{"id":"_T3","span":{"begin":71,"end":78},"obj":"FMAID:82839"},{"id":"_T4","span":{"begin":71,"end":78},"obj":"FMAID:167420"},{"id":"_T5","span":{"begin":118,"end":125},"obj":"FMAID:167420"},{"id":"_T6","span":{"begin":118,"end":125},"obj":"FMAID:82839"},{"id":"_T7","span":{"begin":194,"end":214},"obj":"FMAID:82837"},{"id":"_T8","span":{"begin":194,"end":214},"obj":"FMAID:196838"},{"id":"_T9","span":{"begin":225,"end":232},"obj":"FMAID:165191"},{"id":"_T10","span":{"begin":225,"end":232},"obj":"FMAID:67110"},{"id":"_T11","span":{"begin":225,"end":240},"obj":"FMAID:167405"},{"id":"_T12","span":{"begin":225,"end":240},"obj":"FMAID:63023"},{"id":"_T13","span":{"begin":259,"end":271},"obj":"FMAID:197276"},{"id":"_T14","span":{"begin":259,"end":271},"obj":"FMAID:82737"},{"id":"_T15","span":{"begin":333,"end":339},"obj":"FMAID:50801"},{"id":"_T16","span":{"begin":333,"end":339},"obj":"FMAID:146514"},{"id":"_T17","span":{"begin":358,"end":365},"obj":"FMAID:169646"},{"id":"_T18","span":{"begin":358,"end":365},"obj":"FMAID:69068"},{"id":"_T19","span":{"begin":392,"end":403},"obj":"FMAID:82797"},{"id":"_T21","span":{"begin":417,"end":435},"obj":"FMAID:167395"},{"id":"_T22","span":{"begin":417,"end":435},"obj":"FMAID:63011"},{"id":"_T23","span":{"begin":657,"end":670},"obj":"FMAID:82744"},{"id":"_T24","span":{"begin":657,"end":670},"obj":"FMAID:196733"},{"id":"_T25","span":{"begin":771,"end":792},"obj":"FMAID:82786"},{"id":"_T26","span":{"begin":771,"end":792},"obj":"FMAID:196780"},{"id":"_T27","span":{"begin":919,"end":940},"obj":"FMAID:82786"},{"id":"_T28","span":{"begin":919,"end":940},"obj":"FMAID:196780"},{"id":"_T29","span":{"begin":1123,"end":1138},"obj":"FMAID:82798"},{"id":"_T30","span":{"begin":1123,"end":1138},"obj":"FMAID:196793"},{"id":"_T31","span":{"begin":1244,"end":1257},"obj":"FMAID:82744"},{"id":"_T32","span":{"begin":1244,"end":1257},"obj":"FMAID:196733"},{"id":"_T33","span":{"begin":1521,"end":1528},"obj":"FMAID:167420"},{"id":"_T34","span":{"begin":1521,"end":1528},"obj":"FMAID:82839"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":60,"end":67},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T2","span":{"begin":102,"end":109},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T3","span":{"begin":111,"end":113},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T4","span":{"begin":457,"end":459},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T5","span":{"begin":1073,"end":1075},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T6","span":{"begin":1590,"end":1592},"obj":"http://www.uniprot.org/uniprot/P21741"},{"id":"T7","span":{"begin":111,"end":113},"obj":"http://www.uniprot.org/uniprot/Q03426"},{"id":"T8","span":{"begin":457,"end":459},"obj":"http://www.uniprot.org/uniprot/Q03426"},{"id":"T9","span":{"begin":1073,"end":1075},"obj":"http://www.uniprot.org/uniprot/Q03426"},{"id":"T10","span":{"begin":1590,"end":1592},"obj":"http://www.uniprot.org/uniprot/Q03426"},{"id":"T11","span":{"begin":718,"end":732},"obj":"http://www.uniprot.org/uniprot/P34059"},{"id":"T12","span":{"begin":887,"end":889},"obj":"http://www.uniprot.org/uniprot/O75390"},{"id":"T13","span":{"begin":919,"end":942},"obj":"http://www.uniprot.org/uniprot/P15848"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":60,"end":67},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T2","span":{"begin":102,"end":109},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T3","span":{"begin":111,"end":113},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T4","span":{"begin":457,"end":459},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T5","span":{"begin":1073,"end":1075},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T6","span":{"begin":1590,"end":1592},"obj":"http://www.uniprot.org/uniprot/P12025"},{"id":"T7","span":{"begin":111,"end":113},"obj":"http://www.uniprot.org/uniprot/Q9R008"},{"id":"T8","span":{"begin":457,"end":459},"obj":"http://www.uniprot.org/uniprot/Q9R008"},{"id":"T9","span":{"begin":1073,"end":1075},"obj":"http://www.uniprot.org/uniprot/Q9R008"},{"id":"T10","span":{"begin":1590,"end":1592},"obj":"http://www.uniprot.org/uniprot/Q9R008"},{"id":"T11","span":{"begin":111,"end":113},"obj":"http://www.uniprot.org/uniprot/Q9QZM4"},{"id":"T12","span":{"begin":457,"end":459},"obj":"http://www.uniprot.org/uniprot/Q9QZM4"},{"id":"T13","span":{"begin":1073,"end":1075},"obj":"http://www.uniprot.org/uniprot/Q9QZM4"},{"id":"T14","span":{"begin":1590,"end":1592},"obj":"http://www.uniprot.org/uniprot/Q9QZM4"},{"id":"T15","span":{"begin":718,"end":732},"obj":"http://www.uniprot.org/uniprot/Q571E4"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":348,"end":351},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/82391"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":87,"end":93},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T2","span":{"begin":134,"end":140},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T3","span":{"begin":206,"end":214},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":233,"end":240},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":943,"end":950},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":1110,"end":1119},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":1235,"end":1243},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T8","span":{"begin":718,"end":732},"obj":"http://purl.obolibrary.org/obo/GO_0043890"},{"id":"T9","span":{"begin":1283,"end":1292},"obj":"http://purl.obolibrary.org/obo/GO_0007586"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":49,"end":56},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":79,"end":86},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":126,"end":133},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":314,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":569,"end":576},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":698,"end":705},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":858,"end":865},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":1165,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":1369,"end":1376},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T11","span":{"begin":1414,"end":1421},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T12","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T13","span":{"begin":49,"end":56},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":79,"end":86},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":126,"end":133},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T16","span":{"begin":314,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T17","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T18","span":{"begin":569,"end":576},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":698,"end":705},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T20","span":{"begin":858,"end":865},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T21","span":{"begin":1165,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T22","span":{"begin":1369,"end":1376},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T23","span":{"begin":1414,"end":1421},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T24","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T25","span":{"begin":49,"end":56},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T26","span":{"begin":79,"end":86},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T27","span":{"begin":126,"end":133},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T28","span":{"begin":314,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T29","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T30","span":{"begin":569,"end":576},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T31","span":{"begin":698,"end":705},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T32","span":{"begin":858,"end":865},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T33","span":{"begin":1165,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T34","span":{"begin":1369,"end":1376},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T35","span":{"begin":1414,"end":1421},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T36","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T37","span":{"begin":49,"end":56},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T38","span":{"begin":79,"end":86},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T39","span":{"begin":126,"end":133},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T40","span":{"begin":314,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T41","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T42","span":{"begin":569,"end":576},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T43","span":{"begin":698,"end":705},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T44","span":{"begin":858,"end":865},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T45","span":{"begin":1165,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T46","span":{"begin":1369,"end":1376},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T47","span":{"begin":1414,"end":1421},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T48","span":{"begin":149,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T49","span":{"begin":71,"end":86},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T50","span":{"begin":118,"end":133},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T51","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0019838"},{"id":"T52","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0019838"},{"id":"T53","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0048408"},{"id":"T54","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0048408"},{"id":"T55","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0036458"},{"id":"T56","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0036458"},{"id":"T57","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T58","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T59","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0048406"},{"id":"T60","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0048406"},{"id":"T61","span":{"begin":79,"end":100},"obj":"http://purl.obolibrary.org/obo/GO_0070851"},{"id":"T62","span":{"begin":134,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0070851"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":333,"end":339},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"T2","span":{"begin":358,"end":365},"obj":"http://purl.obolibrary.org/obo/UBERON_0000922"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":259,"end":271},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":1007,"end":1012},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":1056,"end":1067},"obj":"http://edamontology.org/topic_0602"},{"id":"T4","span":{"begin":1466,"end":1473},"obj":"http://edamontology.org/topic_3678"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":18,"end":28},"obj":"http://edamontology.org/data_0883"},{"id":"T2","span":{"begin":180,"end":190},"obj":"http://edamontology.org/data_0883"},{"id":"T3","span":{"begin":180,"end":193},"obj":"http://edamontology.org/data_1070"},{"id":"T4","span":{"begin":259,"end":281},"obj":"http://edamontology.org/data_1462"},{"id":"T5","span":{"begin":272,"end":281},"obj":"http://edamontology.org/data_0883"},{"id":"T6","span":{"begin":619,"end":633},"obj":"http://edamontology.org/data_2140"},{"id":"T7","span":{"begin":892,"end":901},"obj":"http://edamontology.org/data_0883"},{"id":"T8","span":{"begin":1021,"end":1029},"obj":"http://edamontology.org/operation_2945"},{"id":"T9","span":{"begin":1216,"end":1223},"obj":"http://edamontology.org/operation_3432"},{"id":"T10","span":{"begin":1550,"end":1559},"obj":"http://edamontology.org/data_0883"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":333,"end":339},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":358,"end":365},"obj":"http://purl.obolibrary.org/obo/MAT_0000226"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":71,"end":78},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T2","span":{"begin":118,"end":125},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T3","span":{"begin":1521,"end":1528},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T4","span":{"begin":194,"end":205},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T5","span":{"begin":194,"end":214},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":409,"end":416},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":194,"end":205},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":225,"end":240},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":333,"end":339},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":358,"end":365},"obj":"http://purl.obolibrary.org/obo/UBERON_0000922"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":333,"end":339},"obj":"Body_part"},{"id":"T2","span":{"begin":358,"end":365},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000226"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":194,"end":205},"obj":"Glycan"},{"id":"T2","span":{"begin":225,"end":240},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":194,"end":205},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":225,"end":240},"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/EP0086"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":352,"end":357},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1007,"end":1012},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10090"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":333,"end":339},"obj":"Body_part"},{"id":"T2","span":{"begin":358,"end":365},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000226"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1432,"end":1593},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"T9","span":{"begin":1432,"end":1593},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"T9","span":{"begin":1432,"end":1593},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":634},"obj":"Sentence"},{"id":"T5","span":{"begin":635,"end":875},"obj":"Sentence"},{"id":"T6","span":{"begin":876,"end":1020},"obj":"Sentence"},{"id":"T7","span":{"begin":1021,"end":1224},"obj":"Sentence"},{"id":"T8","span":{"begin":1225,"end":1431},"obj":"Sentence"},{"id":"T9","span":{"begin":1432,"end":1593},"obj":"Sentence"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":194,"end":205},"obj":"Glycan"},{"id":"T2","span":{"begin":225,"end":240},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":194,"end":205},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":225,"end":240},"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/EP0086"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":352,"end":357},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1007,"end":1012},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10090"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor.\nMidkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK."}