PubMed:1933955 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":279,"end":288},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":836,"end":845},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":896,"end":905},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":940,"end":949},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A8","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":279,"end":288},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":279,"end":288},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":836,"end":845},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":836,"end":845},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T5","span":{"begin":896,"end":905},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":896,"end":905},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T7","span":{"begin":940,"end":949},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T8","span":{"begin":940,"end":949},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":307,"end":312},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T3","span":{"begin":790,"end":801},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T4","span":{"begin":790,"end":795},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":126,"end":289},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":290,"end":473},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":474,"end":563},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":564,"end":736},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":737,"end":950},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":951,"end":1104},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":289},"obj":"Sentence"},{"id":"T3","span":{"begin":290,"end":473},"obj":"Sentence"},{"id":"T4","span":{"begin":474,"end":563},"obj":"Sentence"},{"id":"T5","span":{"begin":564,"end":736},"obj":"Sentence"},{"id":"T6","span":{"begin":737,"end":950},"obj":"Sentence"},{"id":"T7","span":{"begin":951,"end":1104},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":907,"end":916},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G66481II"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66481II"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T3","span":{"begin":790,"end":801},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":907,"end":916},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G66481II"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66481II"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":576,"end":580},"obj":"Cell"},{"id":"T3","span":{"begin":652,"end":656},"obj":"Cell"},{"id":"T4","span":{"begin":786,"end":801},"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:0000560"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A5","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000562"},{"id":"A6","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000595"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":786,"end":801},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000562"},{"id":"A4","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000595"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":65,"end":79},"obj":"Organism"},{"id":"T2","span":{"begin":146,"end":160},"obj":"Organism"},{"id":"T3","span":{"begin":465,"end":472},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4202"},{"id":"A2","pred":"db_id","subj":"T2","obj":"4202"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3846"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":289},"obj":"Sentence"},{"id":"T3","span":{"begin":290,"end":473},"obj":"Sentence"},{"id":"T4","span":{"begin":474,"end":563},"obj":"Sentence"},{"id":"T5","span":{"begin":564,"end":736},"obj":"Sentence"},{"id":"T6","span":{"begin":737,"end":950},"obj":"Sentence"},{"id":"T7","span":{"begin":951,"end":1104},"obj":"Sentence"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":173,"end":176},"obj":"Lectin"},{"id":"T2","span":{"begin":967,"end":970},"obj":"Lectin"},{"id":"T3","span":{"begin":1028,"end":1031},"obj":"Lectin"},{"id":"T4","span":{"begin":1038,"end":1041},"obj":"Lectin"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"GL_003701"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"GL_003701"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"GL_003701"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"GL_003701"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":786,"end":801},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:9670"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:62845"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":790,"end":801},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":65,"end":79},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":146,"end":160},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":465,"end":472},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4202"},{"id":"A2","pred":"db_id","subj":"T2","obj":"4202"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3846"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":786,"end":801},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000562"},{"id":"A4","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000595"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":1038,"end":1044},"obj":"GL_000814"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":1038,"end":1044},"obj":"GL_000814"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":576,"end":580},"obj":"Cell"},{"id":"T3","span":{"begin":652,"end":656},"obj":"Cell"},{"id":"T4","span":{"begin":786,"end":801},"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:0000560"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000232"},{"id":"A5","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000562"},{"id":"A6","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000595"}],"text":"Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.\nA third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them."}