PubMed:11087713 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":70,"end":89},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":70,"end":89},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":91,"end":325},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":326,"end":707},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":708,"end":850},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":851,"end":924},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":925,"end":1125},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1126,"end":1379},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1380,"end":1613},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":707},"obj":"Sentence"},{"id":"T3","span":{"begin":708,"end":850},"obj":"Sentence"},{"id":"T4","span":{"begin":851,"end":1125},"obj":"Sentence"},{"id":"T5","span":{"begin":1126,"end":1379},"obj":"Sentence"},{"id":"T6","span":{"begin":1380,"end":1613},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":325},"obj":"Sentence"},{"id":"T3","span":{"begin":326,"end":707},"obj":"Sentence"},{"id":"T4","span":{"begin":708,"end":850},"obj":"Sentence"},{"id":"T5","span":{"begin":851,"end":924},"obj":"Sentence"},{"id":"T6","span":{"begin":925,"end":1125},"obj":"Sentence"},{"id":"T7","span":{"begin":1126,"end":1379},"obj":"Sentence"},{"id":"T8","span":{"begin":1380,"end":1613},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":70,"end":89},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":180,"end":186},"obj":"http://purl.obolibrary.org/obo/MAT_0000085"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":241,"end":252},"obj":"http://purl.bioontology.org/ontology/ICD10/H10"},{"id":"T2","span":{"begin":241,"end":252},"obj":"http://purl.bioontology.org/ontology/ICD10/H10.9"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":8,"end":20},"obj":"FMAID:82737"},{"id":"_T2","span":{"begin":8,"end":20},"obj":"FMAID:197276"},{"id":"_T3","span":{"begin":70,"end":89},"obj":"FMAID:196781"},{"id":"_T4","span":{"begin":70,"end":89},"obj":"FMAID:82787"},{"id":"_T5","span":{"begin":118,"end":125},"obj":"FMAID:67257"},{"id":"_T6","span":{"begin":118,"end":125},"obj":"FMAID:165447"},{"id":"_T7","span":{"begin":180,"end":186},"obj":"FMAID:93671"},{"id":"_T8","span":{"begin":180,"end":186},"obj":"FMAID:7196"},{"id":"_T9","span":{"begin":180,"end":186},"obj":"FMAID:188495"},{"id":"_T10","span":{"begin":187,"end":197},"obj":"FMAID:165145"},{"id":"_T11","span":{"begin":291,"end":296},"obj":"FMAID:196724"},{"id":"_T12","span":{"begin":415,"end":420},"obj":"FMAID:196724"},{"id":"_T13","span":{"begin":512,"end":519},"obj":"FMAID:165447"},{"id":"_T14","span":{"begin":512,"end":519},"obj":"FMAID:67257"},{"id":"_T15","span":{"begin":651,"end":656},"obj":"FMAID:68646"},{"id":"_T16","span":{"begin":651,"end":656},"obj":"FMAID:169002"},{"id":"_T17","span":{"begin":743,"end":750},"obj":"FMAID:67257"},{"id":"_T18","span":{"begin":743,"end":750},"obj":"FMAID:165447"},{"id":"_T19","span":{"begin":888,"end":895},"obj":"FMAID:165447"},{"id":"_T20","span":{"begin":888,"end":895},"obj":"FMAID:67257"},{"id":"_T21","span":{"begin":1025,"end":1030},"obj":"FMAID:169002"},{"id":"_T22","span":{"begin":1025,"end":1030},"obj":"FMAID:68646"},{"id":"_T23","span":{"begin":1047,"end":1052},"obj":"FMAID:169002"},{"id":"_T24","span":{"begin":1047,"end":1052},"obj":"FMAID:68646"},{"id":"_T25","span":{"begin":1111,"end":1124},"obj":"FMAID:196772"},{"id":"_T26","span":{"begin":1111,"end":1124},"obj":"FMAID:82779"},{"id":"_T27","span":{"begin":1139,"end":1146},"obj":"FMAID:146300"},{"id":"_T28","span":{"begin":1139,"end":1146},"obj":"FMAID:50594"},{"id":"_T29","span":{"begin":1246,"end":1251},"obj":"FMAID:196724"},{"id":"_T30","span":{"begin":1277,"end":1283},"obj":"FMAID:165145"},{"id":"_T31","span":{"begin":1429,"end":1441},"obj":"FMAID:197276"},{"id":"_T32","span":{"begin":1429,"end":1441},"obj":"FMAID:82737"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":588,"end":619},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T2","span":{"begin":588,"end":619},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T3","span":{"begin":588,"end":619},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T4","span":{"begin":588,"end":623},"obj":"http://www.uniprot.org/uniprot/Q09327"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":588,"end":619},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T2","span":{"begin":588,"end":623},"obj":"http://www.uniprot.org/uniprot/Q10470"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":651,"end":656},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":1025,"end":1030},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":1047,"end":1052},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1359,"end":1362},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T5","span":{"begin":1592,"end":1612},"obj":"http://purl.bioontology.org/ontology/STY/T039"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":21,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0051099"},{"id":"T2","span":{"begin":488,"end":504},"obj":"http://purl.obolibrary.org/obo/GO_0051099"},{"id":"T3","span":{"begin":1442,"end":1458},"obj":"http://purl.obolibrary.org/obo/GO_0051099"},{"id":"T4","span":{"begin":488,"end":519},"obj":"http://purl.obolibrary.org/obo/GO_0032092"},{"id":"T5","span":{"begin":588,"end":623},"obj":"http://purl.obolibrary.org/obo/GO_0003830"},{"id":"T6","span":{"begin":807,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":1520,"end":1527},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":8,"end":28},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":1429,"end":1449},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T3","span":{"begin":21,"end":28},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":110,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":488,"end":495},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":573,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":1067,"end":1074},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":1305,"end":1312},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":406,"end":411},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":992,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T11","span":{"begin":1203,"end":1208},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T12","span":{"begin":21,"end":28},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T13","span":{"begin":110,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":488,"end":495},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":573,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T16","span":{"begin":1067,"end":1074},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T17","span":{"begin":1305,"end":1312},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T18","span":{"begin":406,"end":411},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":992,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T20","span":{"begin":1203,"end":1208},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T21","span":{"begin":21,"end":28},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T22","span":{"begin":110,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T23","span":{"begin":488,"end":495},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T24","span":{"begin":573,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T25","span":{"begin":1067,"end":1074},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T26","span":{"begin":1305,"end":1312},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T27","span":{"begin":406,"end":411},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T28","span":{"begin":992,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T29","span":{"begin":1203,"end":1208},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T30","span":{"begin":21,"end":28},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T31","span":{"begin":110,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T32","span":{"begin":488,"end":495},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T33","span":{"begin":573,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T34","span":{"begin":1067,"end":1074},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T35","span":{"begin":1305,"end":1312},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T36","span":{"begin":406,"end":411},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T37","span":{"begin":992,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T38","span":{"begin":1203,"end":1208},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T39","span":{"begin":110,"end":125},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T40","span":{"begin":406,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T41","span":{"begin":488,"end":519},"obj":"http://purl.obolibrary.org/obo/GO_0032794"},{"id":"T42","span":{"begin":573,"end":589},"obj":"http://purl.obolibrary.org/obo/GO_0005112"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":651,"end":656},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1025,"end":1030},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1047,"end":1052},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":180,"end":186},"obj":"http://purl.obolibrary.org/obo/UBERON_0002106"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":8,"end":20},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":118,"end":125},"obj":"http://edamontology.org/topic_0078"},{"id":"T3","span":{"begin":512,"end":519},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":743,"end":750},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":854,"end":864},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":854,"end":864},"obj":"http://edamontology.org/topic_3168"},{"id":"T7","span":{"begin":854,"end":873},"obj":"http://edamontology.org/topic_0080"},{"id":"T8","span":{"begin":888,"end":895},"obj":"http://edamontology.org/topic_0078"},{"id":"T9","span":{"begin":1372,"end":1378},"obj":"http://edamontology.org/topic_3277"},{"id":"T10","span":{"begin":1429,"end":1441},"obj":"http://edamontology.org/topic_0152"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":118,"end":125},"obj":"http://edamontology.org/format_1208"},{"id":"T2","span":{"begin":118,"end":125},"obj":"http://edamontology.org/data_1467"},{"id":"T3","span":{"begin":512,"end":519},"obj":"http://edamontology.org/format_1208"},{"id":"T4","span":{"begin":512,"end":519},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":712,"end":726},"obj":"http://edamontology.org/data_0844"},{"id":"T6","span":{"begin":743,"end":750},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":743,"end":750},"obj":"http://edamontology.org/format_1208"},{"id":"T8","span":{"begin":854,"end":864},"obj":"http://edamontology.org/data_2044"},{"id":"T9","span":{"begin":854,"end":864},"obj":"http://edamontology.org/operation_3218"},{"id":"T10","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_2408"},{"id":"T11","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_0258"},{"id":"T12","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_3229"},{"id":"T13","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_2404"},{"id":"T14","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_2403"},{"id":"T15","span":{"begin":854,"end":873},"obj":"http://edamontology.org/operation_3197"},{"id":"T16","span":{"begin":865,"end":873},"obj":"http://edamontology.org/operation_2945"},{"id":"T17","span":{"begin":888,"end":895},"obj":"http://edamontology.org/data_1467"},{"id":"T18","span":{"begin":888,"end":895},"obj":"http://edamontology.org/format_1208"},{"id":"T19","span":{"begin":888,"end":910},"obj":"http://edamontology.org/data_0989"},{"id":"T20","span":{"begin":888,"end":910},"obj":"http://edamontology.org/data_1008"},{"id":"T21","span":{"begin":900,"end":910},"obj":"http://edamontology.org/data_0842"},{"id":"T22","span":{"begin":900,"end":910},"obj":"http://edamontology.org/data_2611"},{"id":"T23","span":{"begin":941,"end":949},"obj":"http://edamontology.org/operation_2945"},{"id":"T24","span":{"begin":1165,"end":1177},"obj":"http://edamontology.org/data_3108"},{"id":"T25","span":{"begin":1603,"end":1612},"obj":"http://edamontology.org/operation_0004"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":70,"end":89},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":103,"end":109},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":456,"end":462},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":700,"end":706},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":1541,"end":1547},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":180,"end":186},"obj":"http://purl.obolibrary.org/obo/MAT_0000085"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":41,"end":50},"obj":"https://acgg.asia/db/lfdb/LfDB0008"},{"id":"Lectin_T2","span":{"begin":914,"end":923},"obj":"https://acgg.asia/db/lfdb/LfDB0008"},{"id":"Lectin_T3","span":{"begin":982,"end":991},"obj":"https://acgg.asia/db/lfdb/LfDB0008"},{"id":"Lectin_T4","span":{"begin":1193,"end":1202},"obj":"https://acgg.asia/db/lfdb/LfDB0008"},{"id":"Lectin_T5","span":{"begin":1407,"end":1416},"obj":"https://acgg.asia/db/lfdb/LfDB0008"},{"id":"Lectin_T6","span":{"begin":41,"end":50},"obj":"https://acgg.asia/db/lfdb/LfDB0009"},{"id":"Lectin_T7","span":{"begin":914,"end":923},"obj":"https://acgg.asia/db/lfdb/LfDB0009"},{"id":"Lectin_T8","span":{"begin":982,"end":991},"obj":"https://acgg.asia/db/lfdb/LfDB0009"},{"id":"Lectin_T9","span":{"begin":1193,"end":1202},"obj":"https://acgg.asia/db/lfdb/LfDB0009"},{"id":"Lectin_T10","span":{"begin":1407,"end":1416},"obj":"https://acgg.asia/db/lfdb/LfDB0009"},{"id":"Lectin_T11","span":{"begin":41,"end":50},"obj":"https://acgg.asia/db/lfdb/LfDB0010"},{"id":"Lectin_T12","span":{"begin":914,"end":923},"obj":"https://acgg.asia/db/lfdb/LfDB0010"},{"id":"Lectin_T13","span":{"begin":982,"end":991},"obj":"https://acgg.asia/db/lfdb/LfDB0010"},{"id":"Lectin_T14","span":{"begin":1193,"end":1202},"obj":"https://acgg.asia/db/lfdb/LfDB0010"},{"id":"Lectin_T15","span":{"begin":1407,"end":1416},"obj":"https://acgg.asia/db/lfdb/LfDB0010"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":974,"end":981},"obj":"id"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

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gin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T138","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T139","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T140","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T141","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T142","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T143","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T144","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T145","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T146","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T147","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T148","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T149","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T150","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T151","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T152","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T153","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T154","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T155","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T156","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T157","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T158","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T159","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T160","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T161","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T162","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T163","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T164","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T165","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T166","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T167","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T168","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T169","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T170","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T171","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T172","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T173","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T174","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T175","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T176","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T177","span":{"begin":103,"end":109},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T178","span":{"begin":456,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T179","span":{"begin":700,"end":706},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T180","span":{"begin":1541,"end":1547},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T181","span":{"begin":291,"end":296},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T182","span":{"begin":415,"end":420},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T183","span":{"begin":1246,"end":1251},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T184","span":{"begin":291,"end":296},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T185","span":{"begin":415,"end":420},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T186","span":{"begin":1246,"end":1251},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T187","span":{"begin":291,"end":296},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""},{"id":"GlycanIUPAC_T188","span":{"begin":415,"end":420},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""},{"id":"GlycanIUPAC_T189","span":{"begin":1246,"end":1251},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""},{"id":"GlycanIUPAC_T190","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T191","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T192","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T193","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T194","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T195","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T196","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T197","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T198","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T199","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T200","span":{"begin":1359,"end":1362},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":180,"end":186},"obj":"http://purl.obolibrary.org/obo/UBERON_0002106"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":180,"end":186},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000085"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":379,"end":382},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0007710"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0008214"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":384,"end":390},"obj":"lectin"},{"id":"T2","span":{"begin":566,"end":572},"obj":"lectin"},{"id":"T3","span":{"begin":1490,"end":1496},"obj":"lectin"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":707},"obj":"Sentence"},{"id":"T3","span":{"begin":708,"end":850},"obj":"Sentence"},{"id":"T4","span":{"begin":851,"end":1125},"obj":"Sentence"},{"id":"T5","span":{"begin":1126,"end":1379},"obj":"Sentence"},{"id":"T6","span":{"begin":1380,"end":1613},"obj":"Sentence"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":180,"end":186},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002106"}],"text":"A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine.\nA bisecting GlcNAc-binding protein was purified from a Triton X-100 extract of a porcine spleen microsomal fraction using affinity chromatography, in conjunction with an agalacto bisected biantennary sugar chain-immobilized Sepharose. Since the erythroagglutinating phytohemagglutinin (E-PHA) lectin preferentially binds to sugar chains which contain the bisecting GlcNAc, during purification the binding activity of the protein was evaluated by monitoring the inhibition of lectin binding to the N-acetylglucosaminyltransferase III (GnT-III)-transfected K562 cells which express high levels of the bisecting GlcNAc. The molecular mass of the purified protein was found to be 33 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By sequencing analysis, the isolated protein was identified as annexin V. Flow cytometric analysis showed that fluorescein-labeled annexin V binds to the GnT-III-transfected cells but not to mock cells, and that the binding was not affected by the addition of phospholipids. Furthermore, surface plasmon resonance measurements indicated that annexin V binds to the agalacto bisected biantennary sugar chain with a K(d) of 200 microM while essentially no binding was observed in the case of the corresponding non-bisected sample. These results suggest that annexin V has a novel carbohydrate binding activity and may serve as an endogenous lectin for mediating possible signals of bisecting GlcNAc, which have been implicated in a variety of biological functions."}