PubMed:10561458 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":83,"end":90},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":83,"end":90},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":708,"end":715},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T4","span":{"begin":708,"end":715},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T5","span":{"begin":1124,"end":1131},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T6","span":{"begin":1124,"end":1131},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":83,"end":90},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":708,"end":715},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1124,"end":1131},"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/G54161DR"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00021MO"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":82},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":83,"end":199},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":200,"end":337},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":338,"end":562},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":563,"end":763},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":764,"end":1030},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1031,"end":1273},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1274,"end":1411},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":82},"obj":"Sentence"},{"id":"T2","span":{"begin":83,"end":199},"obj":"Sentence"},{"id":"T3","span":{"begin":200,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":562},"obj":"Sentence"},{"id":"T5","span":{"begin":563,"end":763},"obj":"Sentence"},{"id":"T6","span":{"begin":764,"end":1030},"obj":"Sentence"},{"id":"T7","span":{"begin":1031,"end":1273},"obj":"Sentence"},{"id":"T8","span":{"begin":1274,"end":1411},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":82},"obj":"Sentence"},{"id":"T2","span":{"begin":83,"end":199},"obj":"Sentence"},{"id":"T3","span":{"begin":200,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":562},"obj":"Sentence"},{"id":"T5","span":{"begin":563,"end":763},"obj":"Sentence"},{"id":"T6","span":{"begin":764,"end":1030},"obj":"Sentence"},{"id":"T7","span":{"begin":1031,"end":1273},"obj":"Sentence"},{"id":"T8","span":{"begin":1274,"end":1411},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":83,"end":90},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":83,"end":90},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":708,"end":715},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T4","span":{"begin":708,"end":715},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T5","span":{"begin":1124,"end":1131},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T6","span":{"begin":1124,"end":1131},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":95,"end":110},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":53,"end":70},"obj":"FMAID:63011"},{"id":"_T2","span":{"begin":53,"end":70},"obj":"FMAID:167395"},{"id":"_T3","span":{"begin":83,"end":90},"obj":"FMAID:167420"},{"id":"_T4","span":{"begin":83,"end":90},"obj":"FMAID:82839"},{"id":"_T5","span":{"begin":95,"end":102},"obj":"FMAID:165191"},{"id":"_T6","span":{"begin":95,"end":102},"obj":"FMAID:67110"},{"id":"_T7","span":{"begin":95,"end":110},"obj":"FMAID:63023"},{"id":"_T8","span":{"begin":95,"end":110},"obj":"FMAID:167405"},{"id":"_T9","span":{"begin":115,"end":135},"obj":"FMAID:167966"},{"id":"_T10","span":{"begin":115,"end":135},"obj":"FMAID:50627"},{"id":"_T11","span":{"begin":136,"end":151},"obj":"FMAID:196735"},{"id":"_T12","span":{"begin":136,"end":151},"obj":"FMAID:82746"},{"id":"_T13","span":{"begin":136,"end":151},"obj":"FMAID:196779"},{"id":"_T14","span":{"begin":136,"end":151},"obj":"FMAID:82785"},{"id":"_T15","span":{"begin":302,"end":316},"obj":"FMAID:82746"},{"id":"_T16","span":{"begin":302,"end":316},"obj":"FMAID:196735"},{"id":"_T17","span":{"begin":302,"end":316},"obj":"FMAID:196779"},{"id":"_T18","span":{"begin":302,"end":316},"obj":"FMAID:82785"},{"id":"_T19","span":{"begin":328,"end":336},"obj":"FMAID:165447"},{"id":"_T20","span":{"begin":328,"end":336},"obj":"FMAID:67257"},{"id":"_T21","span":{"begin":389,"end":399},"obj":"FMAID:196733"},{"id":"_T22","span":{"begin":389,"end":399},"obj":"FMAID:82744"},{"id":"_T23","span":{"begin":464,"end":471},"obj":"FMAID:67257"},{"id":"_T24","span":{"begin":464,"end":471},"obj":"FMAID:165447"},{"id":"_T25","span":{"begin":522,"end":536},"obj":"FMAID:82746"},{"id":"_T26","span":{"begin":522,"end":536},"obj":"FMAID:82785"},{"id":"_T27","span":{"begin":522,"end":536},"obj":"FMAID:196735"},{"id":"_T28","span":{"begin":522,"end":536},"obj":"FMAID:196779"},{"id":"_T29","span":{"begin":595,"end":607},"obj":"FMAID:67498"},{"id":"_T30","span":{"begin":595,"end":607},"obj":"FMAID:166081"},{"id":"_T31","span":{"begin":708,"end":715},"obj":"FMAID:167420"},{"id":"_T32","span":{"begin":708,"end":715},"obj":"FMAID:82839"},{"id":"_T33","span":{"begin":796,"end":811},"obj":"FMAID:196731"},{"id":"_T34","span":{"begin":796,"end":811},"obj":"FMAID:82742"},{"id":"_T35","span":{"begin":915,"end":929},"obj":"FMAID:82746"},{"id":"_T36","span":{"begin":915,"end":929},"obj":"FMAID:196735"},{"id":"_T37","span":{"begin":915,"end":929},"obj":"FMAID:196779"},{"id":"_T38","span":{"begin":915,"end":929},"obj":"FMAID:82785"},{"id":"_T39","span":{"begin":1124,"end":1131},"obj":"FMAID:167420"},{"id":"_T40","span":{"begin":1124,"end":1131},"obj":"FMAID:82839"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":128,"end":135},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T2","span":{"begin":631,"end":650},"obj":"http://purl.bioontology.org/ontology/STY/T039"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":71,"end":81},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T2","span":{"begin":690,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T3","span":{"begin":859,"end":868},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T4","span":{"begin":1098,"end":1107},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T5","span":{"begin":103,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":666,"end":675},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T7","span":{"begin":891,"end":902},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T8","span":{"begin":1135,"end":1139},"obj":"http://purl.obolibrary.org/obo/GO_0016152"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":482,"end":489},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":1209,"end":1216},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":482,"end":489},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":1209,"end":1216},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T5","span":{"begin":482,"end":489},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T6","span":{"begin":1209,"end":1216},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T7","span":{"begin":482,"end":489},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T8","span":{"begin":1209,"end":1216},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":708,"end":715},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T2","span":{"begin":1124,"end":1131},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":95,"end":110},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":595,"end":607},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":82},"obj":"Sentence"},{"id":"T2","span":{"begin":83,"end":199},"obj":"Sentence"},{"id":"T3","span":{"begin":200,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":562},"obj":"Sentence"},{"id":"T5","span":{"begin":563,"end":763},"obj":"Sentence"},{"id":"T6","span":{"begin":764,"end":1030},"obj":"Sentence"},{"id":"T7","span":{"begin":1031,"end":1273},"obj":"Sentence"},{"id":"T8","span":{"begin":1274,"end":1411},"obj":"Sentence"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":95,"end":110},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.\nHeparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin."}