PubMed:9870354 JSONTXT

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":118,"end":133},"obj":"Body_part"},{"id":"T2","span":{"begin":199,"end":208},"obj":"Body_part"},{"id":"T3","span":{"begin":243,"end":248},"obj":"Body_part"},{"id":"T4","span":{"begin":271,"end":276},"obj":"Body_part"},{"id":"T5","span":{"begin":955,"end":962},"obj":"Body_part"},{"id":"T6","span":{"begin":1012,"end":1016},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000233"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000233"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000972"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1166,"end":1172},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1166,"end":1172},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1166,"end":1172},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":118,"end":123},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":118,"end":123},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T3","span":{"begin":271,"end":276},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T4","span":{"begin":271,"end":276},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T5","span":{"begin":955,"end":962},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"T6","span":{"begin":1012,"end":1016},"obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":752,"end":758},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T2","span":{"begin":888,"end":894},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T3","span":{"begin":1252,"end":1260},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T4","span":{"begin":1371,"end":1380},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T5","span":{"begin":1429,"end":1437},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos600-GlycoEpitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1185,"end":1187},"obj":"http://www.glycoepitope.jp/epitopes/AN0746"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"PD-FMA-PAE-B_T1","span":{"begin":118,"end":133},"obj":"http://purl.org/sig/ont/fma/fma62851"},{"id":"PD-FMA-PAE-B_T2","span":{"begin":199,"end":208},"obj":"http://purl.org/sig/ont/fma/fma62851"},{"id":"PD-FMA-PAE-B_T3","span":{"begin":243,"end":248},"obj":"http://purl.org/sig/ont/fma/fma63083"},{"id":"PD-FMA-PAE-B_T4","span":{"begin":271,"end":276},"obj":"http://purl.org/sig/ont/fma/fma9670"},{"id":"PD-FMA-PAE-B_T5","span":{"begin":458,"end":470},"obj":"http://purl.org/sig/ont/fma/fma82784"},{"id":"PD-FMA-PAE-B_T6","span":{"begin":558,"end":565},"obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"PD-FMA-PAE-B_T7","span":{"begin":917,"end":932},"obj":"http://purl.org/sig/ont/fma/fma82742"},{"id":"PD-FMA-PAE-B_T8","span":{"begin":1012,"end":1016},"obj":"http://purl.org/sig/ont/fma/fma9712"},{"id":"PD-FMA-PAE-B_T9","span":{"begin":1036,"end":1051},"obj":"http://purl.org/sig/ont/fma/fma82742"},{"id":"PD-FMA-PAE-B_T10","span":{"begin":1142,"end":1154},"obj":"http://purl.org/sig/ont/fma/fma82784"},{"id":"PD-FMA-PAE-B_T11","span":{"begin":1166,"end":1172},"obj":"http://purl.org/sig/ont/fma/fma82790"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":134},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":135,"end":304},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":305,"end":523},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":524,"end":795},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":796,"end":998},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":999,"end":1082},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1083,"end":1209},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1210,"end":1247},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1248,"end":1331},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1332,"end":1438},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":134},"obj":"Sentence"},{"id":"T2","span":{"begin":135,"end":304},"obj":"Sentence"},{"id":"T3","span":{"begin":305,"end":523},"obj":"Sentence"},{"id":"T4","span":{"begin":524,"end":795},"obj":"Sentence"},{"id":"T5","span":{"begin":796,"end":998},"obj":"Sentence"},{"id":"T6","span":{"begin":999,"end":1082},"obj":"Sentence"},{"id":"T7","span":{"begin":1083,"end":1209},"obj":"Sentence"},{"id":"T8","span":{"begin":1210,"end":1247},"obj":"Sentence"},{"id":"T9","span":{"begin":1248,"end":1331},"obj":"Sentence"},{"id":"T10","span":{"begin":1332,"end":1438},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":1166,"end":1172},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa204/trivialname"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":1166,"end":1172},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa204/trivialname"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos600-MAT","denotations":[{"id":"PD-MAT-B_T1","span":{"begin":118,"end":123},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"PD-MAT-B_T2","span":{"begin":271,"end":276},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"PD-MAT-B_T3","span":{"begin":118,"end":123},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"PD-MAT-B_T4","span":{"begin":271,"end":276},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"PD-MAT-B_T5","span":{"begin":1012,"end":1016},"obj":"http://purl.obolibrary.org/obo/MAT_0000091"},{"id":"PD-MAT-B_T6","span":{"begin":955,"end":962},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":446,"end":457},"obj":"http://purl.uniprot.org/uniprot/P12346"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":112,"end":117},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":193,"end":198},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:9606"}],"text":"Purification and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}

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and characterization of GDP-L-Fuc: N-acetyl beta-D-glucosaminide alpha1--\u003e6fucosyltransferase from human blood platelets.\nc-6-L-Fucosyltransferase (alpha1,6FucT; EC 2.4.1.68) from human platelets, the enzyme that is released into serum during coagulation of blood, was purified 100,000-fold. The purification required three sequential chromatographic steps: chromatofocusing, affinity column chromatography on GnGn-Gp(asialo-aglacto-transferrin glycopeptide)-CH-Sepharose, and gel filtration of Sephadex G-200. The final preparation contained a protein that migrated as a single discrete band Mr of 58,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under non-reducing conditions, and as a single enzymatically active peak Mr of 58,000 in gel filtration. Although the purified enzyme utilized the biantennary GnGn-Gp as substrate, it was twice as active with the triantennary oligosaccharide when the Man alpha1,3 antenna was substituted with GlcNacbeta1,4. On the other hand the tetraantennary oligosaccharide was not a preferred substrate. The Km values for the substrate asialo-agalactotransferrin-glycopeptide, and GDP-L-fucose were 29 and 28 microM, respectively. The optimum pH of the enzyme was 6.0. The activity of alpha1,6FucT was abolished in the presence of beta-mercaptoethanol. Divalent cations such as Mg2+ and Ca2+ activated, but Cu2+, Zn2+ and Ni2+ strongly inhibited the activity."}