PubMed:2136348 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":390,"end":409},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":657,"end":676},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":955,"end":974},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1012,"end":1031},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1433,"end":1442},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G56045WU"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46055MA"},{"id":"A7","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G45207BM"},{"id":"A8","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G26929DQ"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1433,"end":1442},"obj":"http://www.glycoepitope.jp/epitopes/EP0138"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":390,"end":409},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":657,"end":676},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":955,"end":974},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T4","span":{"begin":1012,"end":1031},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T5","span":{"begin":1433,"end":1442},"obj":"https://glytoucan.org/Structures/Glycans/G26929DQ"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":129,"end":363},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":364,"end":605},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":606,"end":748},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":749,"end":997},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":998,"end":1202},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1203,"end":1284},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1285,"end":1552},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":363},"obj":"Sentence"},{"id":"T3","span":{"begin":364,"end":605},"obj":"Sentence"},{"id":"T4","span":{"begin":606,"end":748},"obj":"Sentence"},{"id":"T5","span":{"begin":749,"end":997},"obj":"Sentence"},{"id":"T6","span":{"begin":998,"end":1202},"obj":"Sentence"},{"id":"T7","span":{"begin":1203,"end":1284},"obj":"Sentence"},{"id":"T8","span":{"begin":1285,"end":1552},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":452,"end":463},"obj":"HP_0001901"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1433,"end":1442},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G56045WU"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G56045WU"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":363},"obj":"Sentence"},{"id":"T3","span":{"begin":364,"end":605},"obj":"Sentence"},{"id":"T4","span":{"begin":606,"end":997},"obj":"Sentence"},{"id":"T5","span":{"begin":998,"end":1202},"obj":"Sentence"},{"id":"T6","span":{"begin":1203,"end":1284},"obj":"Sentence"},{"id":"T7","span":{"begin":1285,"end":1552},"obj":"Sentence"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1433,"end":1442},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0138"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":85,"end":104},"obj":"Organism"},{"id":"T2","span":{"begin":245,"end":264},"obj":"Organism"},{"id":"T3","span":{"begin":446,"end":451},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3845"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3845"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":452,"end":463},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000232"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":452,"end":463},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:62845"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":85,"end":104},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":245,"end":264},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":446,"end":451},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3845"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3845"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":452,"end":463},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000232"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":385,"end":389},"obj":"Cell"},{"id":"T3","span":{"begin":452,"end":463},"obj":"Cell"},{"id":"T4","span":{"begin":464,"end":468},"obj":"Cell"},{"id":"T5","span":{"begin":652,"end":656},"obj":"Cell"},{"id":"T7","span":{"begin":950,"end":954},"obj":"Cell"},{"id":"T9","span":{"begin":1007,"end":1011},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000560"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A8","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A9","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A10","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Structural requirements for the binding of oligosaccharides to immobilized lectin of Erythrina variegata (Linn) var. orientalis.\nThe structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with Erythrina variegata agglutinin (EVA) were investigated by means of affinity chromatography on an EVA-Sepharose column. Some of the branched poly-N-acetyllactosamine-type oligosaccharides obtained from human erythrocyte band 3 glycoprotein were found to show high affinity to EVA-Sepharose, whereas complex-type oligosaccharides were shown to have low affinity. Hybrid type, oligomannose-type and unbranched poly-N-acetyllactosamine-type oligosaccharides bound very little or not at all to EVA-Sepharose. To further study the carbohydrate-binding specificity of this lectin, we investigated the interaction of immobilized EVA and oligosaccharide fragments obtained through partial hydrolysis from branched poly-N-acetyllactosamine-type oligosaccharides. Branched poly-N-acetyllactosamine-type oligosaccharides were subjected to limited hydrolysis with 0.1% trifluoroacetic acid at 100 degrees C for 40 min and then separated on an amino-bonded silica column. One of pentasaccharides thus prepared strongly bound to the EVA-Sepharose column. Structural analysis of this pentasaccharide showed that the Gal beta 1-4GlcNAc beta 1-3(Gal beta 1-4GlcNAc beta 1-6)Gal sugar sequence, which is an I-antigen determinant, was essential for the high affinity binding of the oligosaccharides to the EVA-Sepharose column."}