PubMed:3928630 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":75,"end":98},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":181,"end":184},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":222,"end":225},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":378,"end":381},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":455,"end":471},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":666,"end":669},"obj":"Glycan_Motif"},{"id":"T13","span":{"begin":821,"end":824},"obj":"Glycan_Motif"},{"id":"T15","span":{"begin":935,"end":938},"obj":"Glycan_Motif"},{"id":"T17","span":{"begin":1005,"end":1008},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G90562PB"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A7","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G84224TW"},{"id":"A9","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G74621DY"},{"id":"A10","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G20420WT"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A12","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A13","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A14","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A15","pred":"image","subj":"T15","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A16","pred":"image","subj":"T15","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A17","pred":"image","subj":"T17","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A18","pred":"image","subj":"T17","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":74},"obj":"Sentence"},{"id":"T2","span":{"begin":75,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":582},"obj":"Sentence"},{"id":"T5","span":{"begin":583,"end":599},"obj":"Sentence"},{"id":"T6","span":{"begin":600,"end":618},"obj":"Sentence"},{"id":"T7","span":{"begin":619,"end":627},"obj":"Sentence"},{"id":"T8","span":{"begin":628,"end":647},"obj":"Sentence"},{"id":"T9","span":{"begin":648,"end":887},"obj":"Sentence"},{"id":"T10","span":{"begin":888,"end":893},"obj":"Sentence"},{"id":"T11","span":{"begin":894,"end":899},"obj":"Sentence"},{"id":"T12","span":{"begin":900,"end":916},"obj":"Sentence"},{"id":"T13","span":{"begin":917,"end":1114},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":74},"obj":"Sentence"},{"id":"T2","span":{"begin":75,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":582},"obj":"Sentence"},{"id":"T5","span":{"begin":583,"end":599},"obj":"Sentence"},{"id":"T6","span":{"begin":600,"end":618},"obj":"Sentence"},{"id":"T7","span":{"begin":619,"end":627},"obj":"Sentence"},{"id":"T8","span":{"begin":628,"end":647},"obj":"Sentence"},{"id":"T9","span":{"begin":648,"end":887},"obj":"Sentence"},{"id":"T10","span":{"begin":888,"end":893},"obj":"Sentence"},{"id":"T11","span":{"begin":894,"end":899},"obj":"Sentence"},{"id":"T12","span":{"begin":900,"end":916},"obj":"Sentence"},{"id":"T13","span":{"begin":917,"end":1114},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":75,"end":98},"obj":"https://glytoucan.org/Structures/Glycans/G90562PB"},{"id":"T2","span":{"begin":181,"end":184},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T3","span":{"begin":181,"end":184},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T4","span":{"begin":222,"end":225},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T5","span":{"begin":222,"end":225},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T6","span":{"begin":378,"end":381},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T7","span":{"begin":378,"end":381},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T8","span":{"begin":455,"end":471},"obj":"https://glytoucan.org/Structures/Glycans/G20420WT"},{"id":"T9","span":{"begin":455,"end":471},"obj":"https://glytoucan.org/Structures/Glycans/G74621DY"},{"id":"T10","span":{"begin":455,"end":471},"obj":"https://glytoucan.org/Structures/Glycans/G84224TW"},{"id":"T11","span":{"begin":666,"end":669},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T12","span":{"begin":666,"end":669},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T13","span":{"begin":821,"end":824},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T14","span":{"begin":821,"end":824},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T15","span":{"begin":935,"end":938},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T16","span":{"begin":935,"end":938},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T17","span":{"begin":1005,"end":1008},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T18","span":{"begin":1005,"end":1008},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":455,"end":471},"obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":563,"end":568},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":742,"end":748},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":563,"end":568},"obj":"Body_part"},{"id":"T2","span":{"begin":742,"end":748},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":181,"end":184},"obj":"Glycan"},{"id":"T2","span":{"begin":213,"end":218},"obj":"Glycan"},{"id":"T3","span":{"begin":222,"end":225},"obj":"Glycan"},{"id":"T4","span":{"begin":378,"end":381},"obj":"Glycan"},{"id":"T5","span":{"begin":455,"end":471},"obj":"Glycan"},{"id":"T6","span":{"begin":491,"end":497},"obj":"Glycan"},{"id":"T7","span":{"begin":666,"end":669},"obj":"Glycan"},{"id":"T8","span":{"begin":821,"end":824},"obj":"Glycan"},{"id":"T9","span":{"begin":935,"end":938},"obj":"Glycan"},{"id":"T10","span":{"begin":1005,"end":1008},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G84224TW"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":455,"end":471},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":559,"end":562},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":738,"end":741},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":774,"end":779},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10114"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10116"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":563,"end":568},"obj":"Body_part"},{"id":"T3","span":{"begin":742,"end":748},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":563,"end":568},"obj":"Body_part"},{"id":"T2","span":{"begin":742,"end":748},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":74},"obj":"Sentence"},{"id":"T2","span":{"begin":75,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":582},"obj":"Sentence"},{"id":"T5","span":{"begin":583,"end":599},"obj":"Sentence"},{"id":"T6","span":{"begin":600,"end":618},"obj":"Sentence"},{"id":"T7","span":{"begin":619,"end":627},"obj":"Sentence"},{"id":"T8","span":{"begin":628,"end":647},"obj":"Sentence"},{"id":"T9","span":{"begin":648,"end":887},"obj":"Sentence"},{"id":"T10","span":{"begin":888,"end":893},"obj":"Sentence"},{"id":"T11","span":{"begin":894,"end":899},"obj":"Sentence"},{"id":"T12","span":{"begin":900,"end":916},"obj":"Sentence"},{"id":"T13","span":{"begin":917,"end":1114},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":74},"obj":"Sentence"},{"id":"T2","span":{"begin":75,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":582},"obj":"Sentence"},{"id":"T5","span":{"begin":583,"end":599},"obj":"Sentence"},{"id":"T6","span":{"begin":600,"end":618},"obj":"Sentence"},{"id":"T7","span":{"begin":619,"end":627},"obj":"Sentence"},{"id":"T8","span":{"begin":628,"end":647},"obj":"Sentence"},{"id":"T9","span":{"begin":648,"end":887},"obj":"Sentence"},{"id":"T10","span":{"begin":888,"end":893},"obj":"Sentence"},{"id":"T11","span":{"begin":894,"end":899},"obj":"Sentence"},{"id":"T12","span":{"begin":900,"end":916},"obj":"Sentence"},{"id":"T13","span":{"begin":917,"end":1114},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":74},"obj":"Sentence"},{"id":"T2","span":{"begin":75,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":647},"obj":"Sentence"},{"id":"T5","span":{"begin":648,"end":916},"obj":"Sentence"},{"id":"T6","span":{"begin":917,"end":1114},"obj":"Sentence"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":181,"end":184},"obj":"Glycan"},{"id":"T2","span":{"begin":213,"end":218},"obj":"Glycan"},{"id":"T3","span":{"begin":222,"end":225},"obj":"Glycan"},{"id":"T4","span":{"begin":378,"end":381},"obj":"Glycan"},{"id":"T5","span":{"begin":455,"end":471},"obj":"Glycan"},{"id":"T6","span":{"begin":491,"end":497},"obj":"Glycan"},{"id":"T7","span":{"begin":666,"end":669},"obj":"Glycan"},{"id":"T8","span":{"begin":821,"end":824},"obj":"Glycan"},{"id":"T9","span":{"begin":935,"end":938},"obj":"Glycan"},{"id":"T10","span":{"begin":1005,"end":1008},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G84224TW"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":455,"end":471},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":559,"end":562},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":738,"end":741},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":774,"end":779},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10114"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10116"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":563,"end":568},"obj":"Body_part"},{"id":"T3","span":{"begin":742,"end":748},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Preparation and enzymatic degradation of monosulfogangliotriaosylceramide.\nGangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism."}