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GlyCosmos6-Glycan-Motif-Image

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":120,"end":129},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":120,"end":129},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":687,"end":696},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T4","span":{"begin":867,"end":877},"obj":"https://glytoucan.org/Structures/Glycans/G00407UJ"},{"id":"T5","span":{"begin":867,"end":877},"obj":"https://glytoucan.org/Structures/Glycans/G21856LC"},{"id":"T6","span":{"begin":874,"end":877},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T7","span":{"begin":874,"end":877},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T8","span":{"begin":1317,"end":1327},"obj":"https://glytoucan.org/Structures/Glycans/G00407UJ"},{"id":"T9","span":{"begin":1317,"end":1327},"obj":"https://glytoucan.org/Structures/Glycans/G21856LC"},{"id":"T10","span":{"begin":1324,"end":1327},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T11","span":{"begin":1324,"end":1327},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T12","span":{"begin":1512,"end":1521},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T13","span":{"begin":1512,"end":1521},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T14","span":{"begin":1632,"end":1641},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T15","span":{"begin":1632,"end":1641},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T16","span":{"begin":1665,"end":1674},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T17","span":{"begin":1665,"end":1674},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T18","span":{"begin":1678,"end":1685},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T19","span":{"begin":1713,"end":1720},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":687,"end":696},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T2","span":{"begin":874,"end":877},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T3","span":{"begin":1324,"end":1327},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":96,"end":241},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":242,"end":326},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":327,"end":499},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":500,"end":1344},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1345,"end":1721},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":326},"obj":"Sentence"},{"id":"T4","span":{"begin":327,"end":499},"obj":"Sentence"},{"id":"T5","span":{"begin":500,"end":1344},"obj":"Sentence"},{"id":"T6","span":{"begin":1345,"end":1721},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":687,"end":696},"obj":"Glycan"},{"id":"T2","span":{"begin":748,"end":754},"obj":"Glycan"},{"id":"T3","span":{"begin":867,"end":877},"obj":"Glycan"},{"id":"T4","span":{"begin":1054,"end":1060},"obj":"Glycan"},{"id":"T5","span":{"begin":1237,"end":1243},"obj":"Glycan"},{"id":"T6","span":{"begin":1295,"end":1301},"obj":"Glycan"},{"id":"T7","span":{"begin":1317,"end":1327},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A8","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A9","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A10","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A11","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A12","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A13","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A14","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":748,"end":754},"obj":"Glycan"},{"id":"T2","span":{"begin":874,"end":877},"obj":"Glycan"},{"id":"T3","span":{"begin":1054,"end":1060},"obj":"Glycan"},{"id":"T4","span":{"begin":1237,"end":1243},"obj":"Glycan"},{"id":"T5","span":{"begin":1295,"end":1301},"obj":"Glycan"},{"id":"T6","span":{"begin":1324,"end":1327},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A8","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A9","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A10","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos-GlycoEpitope

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":687,"end":696},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":874,"end":877},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1324,"end":1327},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":417,"end":422},"obj":"Cell"},{"id":"T2","span":{"begin":429,"end":434},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004124"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-Taxon

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":66,"end":82},"obj":"Organism"},{"id":"T2","span":{"begin":174,"end":190},"obj":"Organism"},{"id":"T3","span":{"begin":1119,"end":1142},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3818"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3818"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3490"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":241},"obj":"Sentence"},{"id":"T3","span":{"begin":242,"end":326},"obj":"Sentence"},{"id":"T4","span":{"begin":327,"end":499},"obj":"Sentence"},{"id":"T5","span":{"begin":500,"end":1344},"obj":"Sentence"},{"id":"T6","span":{"begin":1345,"end":1721},"obj":"Sentence"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-GlycoEpitope

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":687,"end":696},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":874,"end":877},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1324,"end":1327},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-Lectin-Jamboree

{"project":"GlyCosmos15-Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":204,"end":207},"obj":"Lectin"},{"id":"T2","span":{"begin":566,"end":569},"obj":"Lectin"},{"id":"T3","span":{"begin":625,"end":628},"obj":"Lectin"},{"id":"T4","span":{"begin":660,"end":663},"obj":"Lectin"},{"id":"T5","span":{"begin":1110,"end":1117},"obj":"Lectin"},{"id":"T6","span":{"begin":1416,"end":1419},"obj":"Lectin"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"GL_003655"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"GL_003655"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"GL_003655"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"GL_003655"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"GL_002258"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"GL_003655"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":66,"end":82},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":174,"end":190},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1119,"end":1142},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3818"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3818"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3490"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

GlyCosmos15-Lectin

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":1110,"end":1117},"obj":"GL_000029"},{"id":"T2","span":{"begin":1119,"end":1153},"obj":"GL_000029"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

Lectin_test

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":1110,"end":1117},"obj":"GL_000029"},{"id":"T2","span":{"begin":1119,"end":1153},"obj":"GL_000029"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":417,"end":422},"obj":"Cell"},{"id":"T2","span":{"begin":429,"end":434},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004124"}],"text":"Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin.\n2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mM at 15 degrees and delta H and delta S values of -57.04 kJ.mol-1 and -118.1J.mol-1.K-1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as beta-D-Galp-(1----3)-D-GalNAc, beta-D-Galp-(1----3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1----3)-alpha-D-GalpNAc-(1----3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1----3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1----3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1----3)-beta-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose."}