PubMed:10536032 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1481,"end":1494},"obj":"https://glytoucan.org/Structures/Glycans/G17108EX"},{"id":"T2","span":{"begin":1481,"end":1494},"obj":"https://glytoucan.org/Structures/Glycans/G58507AZ"},{"id":"T3","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G00067MO"},{"id":"T4","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G26934CO"},{"id":"T5","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G41865GQ"},{"id":"T6","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G60395SO"},{"id":"T7","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G65112QB"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1481,"end":1494},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1545,"end":1558},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G58507AZ"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G17108EX"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65112QB"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G60395SO"},{"id":"A5","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G41865GQ"},{"id":"A6","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G26934CO"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00067MO"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1481,"end":1494},"obj":"https://glytoucan.org/Structures/Glycans/G17108EX"},{"id":"T2","span":{"begin":1481,"end":1494},"obj":"https://glytoucan.org/Structures/Glycans/G58507AZ"},{"id":"T3","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G00067MO"},{"id":"T4","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G26934CO"},{"id":"T5","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G41865GQ"},{"id":"T6","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G60395SO"},{"id":"T7","span":{"begin":1545,"end":1558},"obj":"https://glytoucan.org/Structures/Glycans/G65112QB"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T3","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T4","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T5","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":220,"end":232},"obj":"HP_0003003"},{"id":"T2","span":{"begin":220,"end":232},"obj":"HP_0100273"},{"id":"T3","span":{"begin":226,"end":232},"obj":"HP_0002664"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":220,"end":225},"obj":"FMAID:14543"},{"id":"_T2","span":{"begin":220,"end":225},"obj":"FMAID:104231"},{"id":"_T3","span":{"begin":431,"end":445},"obj":"FMAID:82782"},{"id":"_T4","span":{"begin":431,"end":445},"obj":"FMAID:196776"},{"id":"_T5","span":{"begin":613,"end":625},"obj":"FMAID:62925"},{"id":"_T6","span":{"begin":613,"end":625},"obj":"FMAID:167256"},{"id":"_T7","span":{"begin":691,"end":704},"obj":"FMAID:167256"},{"id":"_T8","span":{"begin":691,"end":704},"obj":"FMAID:62925"},{"id":"_T9","span":{"begin":705,"end":711},"obj":"FMAID:178661"},{"id":"_T10","span":{"begin":746,"end":759},"obj":"FMAID:62925"},{"id":"_T11","span":{"begin":746,"end":759},"obj":"FMAID:167256"},{"id":"_T12","span":{"begin":918,"end":924},"obj":"FMAID:178661"},{"id":"_T13","span":{"begin":1090,"end":1104},"obj":"FMAID:196730"},{"id":"_T14","span":{"begin":1090,"end":1104},"obj":"FMAID:82741"},{"id":"_T15","span":{"begin":1138,"end":1154},"obj":"FMAID:196731"},{"id":"_T16","span":{"begin":1138,"end":1154},"obj":"FMAID:82742"},{"id":"_T17","span":{"begin":1221,"end":1227},"obj":"FMAID:183397"},{"id":"_T18","span":{"begin":1235,"end":1251},"obj":"FMAID:196731"},{"id":"_T19","span":{"begin":1235,"end":1251},"obj":"FMAID:82742"},{"id":"_T20","span":{"begin":1256,"end":1271},"obj":"FMAID:196730"},{"id":"_T21","span":{"begin":1256,"end":1271},"obj":"FMAID:82741"},{"id":"_T22","span":{"begin":1272,"end":1278},"obj":"FMAID:178661"},{"id":"_T23","span":{"begin":1481,"end":1486},"obj":"FMAID:256053"},{"id":"_T24","span":{"begin":1545,"end":1550},"obj":"FMAID:256053"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":176,"end":178},"obj":"http://www.uniprot.org/uniprot/P15104"},{"id":"T2","span":{"begin":421,"end":423},"obj":"http://www.uniprot.org/uniprot/P15104"},{"id":"T3","span":{"begin":873,"end":875},"obj":"http://www.uniprot.org/uniprot/P15104"},{"id":"T4","span":{"begin":1054,"end":1056},"obj":"http://www.uniprot.org/uniprot/P15104"},{"id":"T5","span":{"begin":1311,"end":1313},"obj":"http://www.uniprot.org/uniprot/P15104"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":176,"end":178},"obj":"http://www.uniprot.org/uniprot/P15105"},{"id":"T2","span":{"begin":421,"end":423},"obj":"http://www.uniprot.org/uniprot/P15105"},{"id":"T3","span":{"begin":873,"end":875},"obj":"http://www.uniprot.org/uniprot/P15105"},{"id":"T4","span":{"begin":1054,"end":1056},"obj":"http://www.uniprot.org/uniprot/P15105"},{"id":"T5","span":{"begin":1311,"end":1313},"obj":"http://www.uniprot.org/uniprot/P15105"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":63,"end":72},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3849"},{"id":"T2","span":{"begin":63,"end":87},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3850"},{"id":"T3","span":{"begin":74,"end":87},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/941451"},{"id":"T4","span":{"begin":126,"end":135},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3849"},{"id":"T5","span":{"begin":126,"end":150},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3850"},{"id":"T6","span":{"begin":137,"end":150},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/941451"},{"id":"T7","span":{"begin":226,"end":232},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T8","span":{"begin":325,"end":329},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9605"},{"id":"T9","span":{"begin":761,"end":770},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/96820"},{"id":"T10","span":{"begin":1487,"end":1492},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T11","span":{"begin":1551,"end":1556},"obj":"http://purl.bioontology.org/ontology/STY/T096"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":114,"end":305},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":306,"end":394},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":395,"end":639},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":640,"end":1053},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1054,"end":1155},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1156,"end":1228},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1229,"end":1353},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1354,"end":1570},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":305},"obj":"Sentence"},{"id":"T3","span":{"begin":306,"end":394},"obj":"Sentence"},{"id":"T4","span":{"begin":395,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":1053},"obj":"Sentence"},{"id":"T6","span":{"begin":1054,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1228},"obj":"Sentence"},{"id":"T8","span":{"begin":1229,"end":1353},"obj":"Sentence"},{"id":"T9","span":{"begin":1354,"end":1570},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":305},"obj":"Sentence"},{"id":"T3","span":{"begin":306,"end":394},"obj":"Sentence"},{"id":"T4","span":{"begin":395,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":1053},"obj":"Sentence"},{"id":"T6","span":{"begin":1054,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1228},"obj":"Sentence"},{"id":"T8","span":{"begin":1229,"end":1353},"obj":"Sentence"},{"id":"T9","span":{"begin":1354,"end":1570},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":176,"end":180},"obj":"http://purl.obolibrary.org/obo/GO_0016760"},{"id":"T2","span":{"begin":421,"end":425},"obj":"http://purl.obolibrary.org/obo/GO_0016760"},{"id":"T3","span":{"begin":873,"end":877},"obj":"http://purl.obolibrary.org/obo/GO_0016760"},{"id":"T4","span":{"begin":1054,"end":1058},"obj":"http://purl.obolibrary.org/obo/GO_0016760"},{"id":"T5","span":{"begin":1311,"end":1315},"obj":"http://purl.obolibrary.org/obo/GO_0016760"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":1300,"end":1307},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":1300,"end":1307},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":1300,"end":1307},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":1300,"end":1307},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":233,"end":237},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T2","span":{"begin":787,"end":797},"obj":"http://purl.obolibrary.org/obo/UBERON_2001275"},{"id":"T3","span":{"begin":787,"end":797},"obj":"http://purl.obolibrary.org/obo/UBERON_0011268"},{"id":"T4","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T5","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":214,"end":219},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":226,"end":232},"obj":"http://edamontology.org/topic_2640"},{"id":"T3","span":{"begin":446,"end":458},"obj":"http://edamontology.org/topic_0602"},{"id":"T4","span":{"begin":613,"end":638},"obj":"http://edamontology.org/topic_0128"},{"id":"T5","span":{"begin":626,"end":638},"obj":"http://edamontology.org/topic_0602"},{"id":"T6","span":{"begin":645,"end":650},"obj":"http://edamontology.org/topic_3678"},{"id":"T7","span":{"begin":1026,"end":1037},"obj":"http://edamontology.org/topic_0602"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":655,"end":667},"obj":"http://edamontology.org/operation_2246"},{"id":"T2","span":{"begin":1090,"end":1104},"obj":"http://edamontology.org/data_2746"},{"id":"T3","span":{"begin":1235,"end":1271},"obj":"http://edamontology.org/data_2898"},{"id":"T4","span":{"begin":1256,"end":1271},"obj":"http://edamontology.org/data_2746"},{"id":"T5","span":{"begin":1326,"end":1335},"obj":"http://edamontology.org/data_2589"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T3","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T4","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T5","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":1481,"end":1492},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"},{"id":"T2","span":{"begin":1545,"end":1556},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"},{"id":"T3","span":{"begin":1527,"end":1543},"obj":"http://rdf.glycoinfo.org/glycan/G00046MO"},{"id":"T4","span":{"begin":1545,"end":1558},"obj":"http://rdf.glycoinfo.org/glycan/G00067MO"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":176,"end":180},"obj":"https://acgg.asia/db/lfdb/LfDB0223"},{"id":"Lectin_T2","span":{"begin":421,"end":425},"obj":"https://acgg.asia/db/lfdb/LfDB0223"},{"id":"Lectin_T3","span":{"begin":873,"end":877},"obj":"https://acgg.asia/db/lfdb/LfDB0223"},{"id":"Lectin_T4","span":{"begin":1054,"end":1058},"obj":"https://acgg.asia/db/lfdb/LfDB0223"},{"id":"Lectin_T5","span":{"begin":1311,"end":1315},"obj":"https://acgg.asia/db/lfdb/LfDB0223"},{"id":"Lectin_T6","span":{"begin":677,"end":679},"obj":"https://acgg.asia/db/lfdb/LfDB0021"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

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AC_T180","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T181","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T182","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T183","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T184","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T185","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T186","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T187","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T188","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T189","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T190","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T191","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T192","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T193","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T194","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T195","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T196","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T197","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T198","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T199","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T200","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T201","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T202","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T203","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T204","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T205","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T206","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T207","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T208","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T209","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T210","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T211","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T212","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T213","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T214","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T215","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T216","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T217","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T218","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T219","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T220","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T221","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T222","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T223","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T224","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T225","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T226","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T227","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T228","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T229","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T230","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T231","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T232","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T233","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T234","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T235","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T236","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T237","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T238","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T239","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T240","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T241","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T242","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T243","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T244","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T245","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T246","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T247","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T248","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T249","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T250","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T251","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T252","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T253","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T254","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T255","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T256","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T257","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T258","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T259","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T260","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T261","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T262","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T263","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T264","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T265","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T266","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T267","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T268","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T269","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T270","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T271","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T272","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T273","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T274","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T275","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T276","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T277","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T278","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T279","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T280","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T281","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T282","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T283","span":{"begin":1476,"end":1479},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""},{"id":"GlycanIUPAC_T284","span":{"begin":1566,"end":1569},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":220,"end":225},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1481,"end":1486},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1545,"end":1550},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":787,"end":797},"obj":"http://purl.obolibrary.org/obo/UBERON_2001275"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":787,"end":797},"obj":"http://purl.obolibrary.org/obo/UBERON_0011268"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":835,"end":848},"obj":"http://purl.obolibrary.org/obo/UBERON_0001736"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1105,"end":1111},"obj":"Glycan"},{"id":"T2","span":{"begin":1481,"end":1494},"obj":"Glycan"},{"id":"T3","span":{"begin":1499,"end":1505},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A4","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/G00066MO"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00066MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":220,"end":232},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"Body_part"},{"id":"T2","span":{"begin":1481,"end":1486},"obj":"Body_part"},{"id":"T4","span":{"begin":1545,"end":1550},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A3","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"A5","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":220,"end":232},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003003"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1105,"end":1111},"obj":"Glycan"},{"id":"T2","span":{"begin":1499,"end":1505},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A3","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/G39738WL"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":220,"end":232},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003003"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":226,"end":237},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001064"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":220,"end":232},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0002032"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"MONDO:0005575"},{"id":"A3","pred":"mondo_id","subj":"T1","obj":"MONDO:0021063"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"Body_part"},{"id":"T2","span":{"begin":1221,"end":1227},"obj":"Body_part"},{"id":"T3","span":{"begin":1481,"end":1486},"obj":"Body_part"},{"id":"T4","span":{"begin":1545,"end":1550},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002553"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":62,"end":87},"obj":"Organism"},{"id":"T2","span":{"begin":125,"end":150},"obj":"Organism"},{"id":"T3","span":{"begin":214,"end":219},"obj":"Organism"},{"id":"T4","span":{"begin":727,"end":736},"obj":"Organism"},{"id":"T5","span":{"begin":761,"end":770},"obj":"Organism"},{"id":"T6","span":{"begin":814,"end":820},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3850"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3850"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"40674"},{"id":"A5","pred":"db_id","subj":"T5","obj":"96820"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9913"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":305},"obj":"Sentence"},{"id":"T3","span":{"begin":306,"end":394},"obj":"Sentence"},{"id":"T4","span":{"begin":395,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":1053},"obj":"Sentence"},{"id":"T6","span":{"begin":1054,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1228},"obj":"Sentence"},{"id":"T8","span":{"begin":1229,"end":1353},"obj":"Sentence"},{"id":"T9","span":{"begin":1354,"end":1570},"obj":"Sentence"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":88,"end":94},"obj":"lectin"},{"id":"T2","span":{"begin":151,"end":157},"obj":"lectin"},{"id":"T3","span":{"begin":259,"end":265},"obj":"lectin"},{"id":"T4","span":{"begin":505,"end":511},"obj":"lectin"},{"id":"T5","span":{"begin":606,"end":612},"obj":"lectin"},{"id":"T6","span":{"begin":1046,"end":1052},"obj":"lectin"},{"id":"T7","span":{"begin":1201,"end":1207},"obj":"lectin"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":305},"obj":"Sentence"},{"id":"T3","span":{"begin":306,"end":394},"obj":"Sentence"},{"id":"T4","span":{"begin":395,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":1053},"obj":"Sentence"},{"id":"T6","span":{"begin":1054,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1228},"obj":"Sentence"},{"id":"T8","span":{"begin":1229,"end":1353},"obj":"Sentence"},{"id":"T9","span":{"begin":1354,"end":1570},"obj":"Sentence"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"Body_part"},{"id":"T2","span":{"begin":1481,"end":1486},"obj":"Body_part"},{"id":"T3","span":{"begin":1545,"end":1550},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:14543"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:9670"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:9670"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"Body_part"},{"id":"T2","span":{"begin":1481,"end":1486},"obj":"Body_part"},{"id":"T3","span":{"begin":1545,"end":1550},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":62,"end":87},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":125,"end":150},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":214,"end":219},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":325,"end":329},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":761,"end":770},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":814,"end":820},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3850"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3850"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9605"},{"id":"A5","pred":"db_id","subj":"T5","obj":"96820"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9913"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":220,"end":225},"obj":"Body_part"},{"id":"T2","span":{"begin":1221,"end":1227},"obj":"Body_part"},{"id":"T3","span":{"begin":1481,"end":1486},"obj":"Body_part"},{"id":"T4","span":{"begin":1545,"end":1550},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002553"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":226,"end":237},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001064"}],"text":"Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).\nBandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4)(GS I-A(4)), which is cytotoxic to the human colon cancer cell lines, is one of two lectin families derived from its seed extract. It contains only a homo-oligomer of subunit A, and is most specific for GalNAcalpha1--\u003e. In order to elucidate the GS I-A(4)-glycoconjugate interactions in greater detail, the combining site of this lectin was further characterized by enzyme linked lectino-sorbent assay (ELLSA) and by inhibition of lectin-glycoprotein interactions. This study has demonstrated that the Tn-containing glycoproteins tested, consisting of mammalian salivary glycoproteins (armadillo, asialo-hamster sublingual, asialo-ovine, -bovine, and -porcine submandibular), are bound strongly by GS I-A(4.)Among monovalent inhibitors so far tested, p-NO2-phenylalphaGalNAc is the most potent, suggesting that hydrophobic forces are important in the interaction of this lectin. GS I-A(4)is able to accommodate the monosaccharide GalNAc at the nonreducing end of oligosaccharides. This suggests that the combining site of the lectin is a shallow cavity. Among oligosaccharides and monosaccharides tested as inhibitors of the binding of GS I-A(4), the hierarchy of potencies are: GalNAcalpha1--\u003e3GalNAcbeta1--\u003e3Galalpha1--\u003e4Galbeta 1--\u003e4Glc (Forssman pentasaccharide) \u003e GalNAcalpha1--\u003e3(LFucalpha1--\u003e2)Gal (blood group A)()\u003e GalNAc \u003e Galalpha1--\u003e4Gal \u003e Galalpha1--\u003e3Gal (blood group B-like)\u003e Gal."}