PubMed:1158883 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":133,"end":146},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65112QB"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G60395SO"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G41865GQ"},{"id":"A4","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G26934CO"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00067MO"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":438},"obj":"Sentence"},{"id":"T3","span":{"begin":439,"end":587},"obj":"Sentence"},{"id":"T4","span":{"begin":588,"end":638},"obj":"Sentence"},{"id":"T5","span":{"begin":639,"end":827},"obj":"Sentence"},{"id":"T6","span":{"begin":828,"end":922},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":438},"obj":"Sentence"},{"id":"T3","span":{"begin":439,"end":587},"obj":"Sentence"},{"id":"T4","span":{"begin":588,"end":638},"obj":"Sentence"},{"id":"T5","span":{"begin":639,"end":827},"obj":"Sentence"},{"id":"T6","span":{"begin":828,"end":922},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":133,"end":146},"obj":"https://glytoucan.org/Structures/Glycans/G00067MO"},{"id":"T2","span":{"begin":133,"end":146},"obj":"https://glytoucan.org/Structures/Glycans/G26934CO"},{"id":"T3","span":{"begin":133,"end":146},"obj":"https://glytoucan.org/Structures/Glycans/G41865GQ"},{"id":"T4","span":{"begin":133,"end":146},"obj":"https://glytoucan.org/Structures/Glycans/G60395SO"},{"id":"T5","span":{"begin":133,"end":146},"obj":"https://glytoucan.org/Structures/Glycans/G65112QB"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":133,"end":138},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":133,"end":138},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":133,"end":138},"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"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":12,"end":20},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":94,"end":102},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":682,"end":687},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"124307"},{"id":"A2","pred":"db_id","subj":"T2","obj":"124307"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":438},"obj":"Sentence"},{"id":"T3","span":{"begin":439,"end":587},"obj":"Sentence"},{"id":"T4","span":{"begin":588,"end":638},"obj":"Sentence"},{"id":"T5","span":{"begin":639,"end":827},"obj":"Sentence"},{"id":"T6","span":{"begin":828,"end":922},"obj":"Sentence"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":133,"end":138},"obj":"Body_part"},{"id":"T2","span":{"begin":690,"end":701},"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"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":690,"end":701},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000232"}],"text":"Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.\nEquilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins."}