PubMed:1794038 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":817,"end":824},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":817,"end":824},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":87},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":88,"end":332},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":333,"end":654},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":655,"end":716},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":717,"end":851},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":852,"end":965},"obj":"Sentence"},{"id":"T4","span":{"begin":655,"end":716},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":87},"obj":"Sentence"},{"id":"T2","span":{"begin":88,"end":332},"obj":"Sentence"},{"id":"T3","span":{"begin":333,"end":654},"obj":"Sentence"},{"id":"T5","span":{"begin":717,"end":851},"obj":"Sentence"},{"id":"T6","span":{"begin":852,"end":965},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":87},"obj":"Sentence"},{"id":"T2","span":{"begin":88,"end":332},"obj":"Sentence"},{"id":"T3","span":{"begin":333,"end":654},"obj":"Sentence"},{"id":"T4","span":{"begin":655,"end":716},"obj":"Sentence"},{"id":"T5","span":{"begin":717,"end":851},"obj":"Sentence"},{"id":"T6","span":{"begin":852,"end":965},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":817,"end":824},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":389,"end":400},"obj":"http://purl.bioontology.org/ontology/ICD10/H10"},{"id":"T2","span":{"begin":389,"end":400},"obj":"http://purl.bioontology.org/ontology/ICD10/H10.9"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":20,"end":35},"obj":"FMAID:196731"},{"id":"_T2","span":{"begin":20,"end":35},"obj":"FMAID:82742"},{"id":"_T3","span":{"begin":93,"end":108},"obj":"FMAID:82742"},{"id":"_T4","span":{"begin":93,"end":108},"obj":"FMAID:196731"},{"id":"_T5","span":{"begin":583,"end":595},"obj":"FMAID:196792"},{"id":"_T6","span":{"begin":583,"end":595},"obj":"FMAID:82797"},{"id":"_T7","span":{"begin":597,"end":607},"obj":"FMAID:82750"},{"id":"_T8","span":{"begin":597,"end":607},"obj":"FMAID:196739"},{"id":"_T9","span":{"begin":817,"end":824},"obj":"FMAID:82801"},{"id":"_T10","span":{"begin":817,"end":824},"obj":"FMAID:196796"},{"id":"_T11","span":{"begin":825,"end":835},"obj":"FMAID:196739"},{"id":"_T12","span":{"begin":825,"end":835},"obj":"FMAID:82750"},{"id":"_T13","span":{"begin":880,"end":896},"obj":"FMAID:196731"},{"id":"_T14","span":{"begin":880,"end":896},"obj":"FMAID:82742"},{"id":"_T15","span":{"begin":948,"end":964},"obj":"FMAID:196731"},{"id":"_T16","span":{"begin":948,"end":964},"obj":"FMAID:82742"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":528,"end":530},"obj":"http://www.uniprot.org/uniprot/Q9UCA1"},{"id":"T2","span":{"begin":722,"end":724},"obj":"http://www.uniprot.org/uniprot/Q9UCA1"},{"id":"T3","span":{"begin":857,"end":859},"obj":"http://www.uniprot.org/uniprot/Q9UCA1"},{"id":"T4","span":{"begin":528,"end":530},"obj":"http://www.uniprot.org/uniprot/Q9UNY4"},{"id":"T5","span":{"begin":722,"end":724},"obj":"http://www.uniprot.org/uniprot/Q9UNY4"},{"id":"T6","span":{"begin":857,"end":859},"obj":"http://www.uniprot.org/uniprot/Q9UNY4"},{"id":"T7","span":{"begin":535,"end":537},"obj":"http://www.uniprot.org/uniprot/P13726"},{"id":"T8","span":{"begin":734,"end":736},"obj":"http://www.uniprot.org/uniprot/P13726"},{"id":"T9","span":{"begin":911,"end":913},"obj":"http://www.uniprot.org/uniprot/P13726"},{"id":"T10","span":{"begin":617,"end":623},"obj":"http://www.uniprot.org/uniprot/Q96IV0"},{"id":"T11","span":{"begin":674,"end":680},"obj":"http://www.uniprot.org/uniprot/Q96IV0"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":528,"end":530},"obj":"http://www.uniprot.org/uniprot/P19221"},{"id":"T2","span":{"begin":722,"end":724},"obj":"http://www.uniprot.org/uniprot/P19221"},{"id":"T3","span":{"begin":857,"end":859},"obj":"http://www.uniprot.org/uniprot/P19221"},{"id":"T4","span":{"begin":535,"end":537},"obj":"http://www.uniprot.org/uniprot/P20352"},{"id":"T5","span":{"begin":734,"end":736},"obj":"http://www.uniprot.org/uniprot/P20352"},{"id":"T6","span":{"begin":911,"end":913},"obj":"http://www.uniprot.org/uniprot/P20352"},{"id":"T7","span":{"begin":617,"end":623},"obj":"http://www.uniprot.org/uniprot/Q9JI78"},{"id":"T8","span":{"begin":674,"end":680},"obj":"http://www.uniprot.org/uniprot/Q9JI78"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/91382"},{"id":"T2","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/69322"},{"id":"T3","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/239"},{"id":"T4","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/344881"},{"id":"T5","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/200644"},{"id":"T6","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/178355"},{"id":"T7","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/117743"},{"id":"T8","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/312277"},{"id":"T9","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/237"},{"id":"T10","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/387094"},{"id":"T11","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1236486"},{"id":"T12","span":{"begin":56,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/395087"},{"id":"T13","span":{"begin":187,"end":191},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T14","span":{"begin":187,"end":191},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T15","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/312277"},{"id":"T16","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/91382"},{"id":"T17","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/237"},{"id":"T18","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/387094"},{"id":"T19","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/117743"},{"id":"T20","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1236486"},{"id":"T21","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/239"},{"id":"T22","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/178355"},{"id":"T23","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/69322"},{"id":"T24","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/344881"},{"id":"T25","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/395087"},{"id":"T26","span":{"begin":301,"end":315},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/200644"},{"id":"T27","span":{"begin":576,"end":580},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T28","span":{"begin":576,"end":580},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":426,"end":434},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T2","span":{"begin":617,"end":623},"obj":"http://purl.obolibrary.org/obo/GO_0000224"},{"id":"T3","span":{"begin":674,"end":680},"obj":"http://purl.obolibrary.org/obo/GO_0000224"},{"id":"T4","span":{"begin":617,"end":625},"obj":"http://purl.obolibrary.org/obo/GO_0000224"},{"id":"T5","span":{"begin":674,"end":682},"obj":"http://purl.obolibrary.org/obo/GO_0000224"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":359,"end":370},"obj":"http://edamontology.org/topic_0602"},{"id":"T2","span":{"begin":556,"end":563},"obj":"http://edamontology.org/topic_0154"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":235,"end":245},"obj":"http://edamontology.org/data_2611"},{"id":"T2","span":{"begin":235,"end":245},"obj":"http://edamontology.org/data_0842"},{"id":"T3","span":{"begin":556,"end":563},"obj":"http://edamontology.org/data_2906"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":567,"end":595},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":617,"end":623},"obj":"hgnc:17646"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":674,"end":680},"obj":"hgnc:17646"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":182,"end":213},"obj":"hgnc:24622"}],"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":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":812,"end":824},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":221,"end":223},"obj":"http://www.glycoepitope.jp/epitopes/AN0591"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":524,"end":526},"obj":"http://www.glycoepitope.jp/epitopes/AN0591"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":692,"end":694},"obj":"http://www.glycoepitope.jp/epitopes/AN0591"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":56,"end":86},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":301,"end":331},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"238"},{"id":"A2","pred":"db_id","subj":"T2","obj":"238"}],"text":"Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum.\nFour oligosaccharide chain-cleaving enzymes, including two new endoglycosidases distinct from endo-beta-acetylglucosaminidase (Endo) F1, have been identified and purified to homogeneity from cultural filtrates of Flavobacterium meningosepticum. FPLC-directed hydrophobic-interaction chromatography in conjunction with high-resolution ion-exchange chromatography provided a more simple, rapid method for the isolation of endoglycosidase F1, F2 and F3, and the amidase, peptide-N4-N-acetyl-beta-D-glucosaminyl)-asparagine amidase (PNGase F), in greater than 50% yield. The specificity of PNGase F and Endo F1 are well established. Endo F2 and Endo F3 represent new distinct endoglycosidases that prefer complex as compared to high-mannose asparagine-linked glycans. Endo F2 cleaved biantennary oligosaccharides, whereas Endo F3 cleaved both bi- and triantennary oligosaccharides."}