PubMed:1823162 JSON TXT

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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":299,"end":302},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T2","span":{"begin":299,"end":302},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T3","span":{"begin":376,"end":379},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T4","span":{"begin":376,"end":379},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T5","span":{"begin":413,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G46677TE"},{"id":"T6","span":{"begin":413,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G69277LC"},{"id":"T7","span":{"begin":419,"end":423},"obj":"https://glytoucan.org/Structures/Glycans/G37184KW"},{"id":"T8","span":{"begin":419,"end":423},"obj":"https://glytoucan.org/Structures/Glycans/G97612UN"},{"id":"T9","span":{"begin":425,"end":429},"obj":"https://glytoucan.org/Structures/Glycans/G05952XV"},{"id":"T10","span":{"begin":425,"end":429},"obj":"https://glytoucan.org/Structures/Glycans/G40183QN"},{"id":"T11","span":{"begin":435,"end":439},"obj":"https://glytoucan.org/Structures/Glycans/G17077FL"},{"id":"T12","span":{"begin":435,"end":439},"obj":"https://glytoucan.org/Structures/Glycans/G18625KA"},{"id":"T13","span":{"begin":1180,"end":1183},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T14","span":{"begin":1180,"end":1183},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T15","span":{"begin":1250,"end":1253},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T16","span":{"begin":1250,"end":1253},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T17","span":{"begin":1257,"end":1260},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T18","span":{"begin":1257,"end":1260},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T19","span":{"begin":1372,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T20","span":{"begin":1372,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlyCosmos6-Glycan-Motif-Image

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T2","span":{"begin":53,"end":59},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T3","span":{"begin":146,"end":160},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T4","span":{"begin":154,"end":160},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T5","span":{"begin":807,"end":822},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T6","span":{"begin":816,"end":822},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T7","span":{"begin":830,"end":844},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T8","span":{"begin":838,"end":844},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T9","span":{"begin":929,"end":944},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T10","span":{"begin":938,"end":944},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T11","span":{"begin":1076,"end":1091},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T12","span":{"begin":1085,"end":1091},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T13","span":{"begin":1426,"end":1441},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T14","span":{"begin":1435,"end":1441},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T15","span":{"begin":1690,"end":1696},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T16","span":{"begin":1821,"end":1827},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

sentences

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":299,"end":302},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T2","span":{"begin":299,"end":302},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T3","span":{"begin":376,"end":379},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T4","span":{"begin":376,"end":379},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T5","span":{"begin":413,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G46677TE"},{"id":"T6","span":{"begin":413,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G69277LC"},{"id":"T7","span":{"begin":419,"end":423},"obj":"https://glytoucan.org/Structures/Glycans/G37184KW"},{"id":"T8","span":{"begin":419,"end":423},"obj":"https://glytoucan.org/Structures/Glycans/G97612UN"},{"id":"T9","span":{"begin":425,"end":429},"obj":"https://glytoucan.org/Structures/Glycans/G05952XV"},{"id":"T10","span":{"begin":425,"end":429},"obj":"https://glytoucan.org/Structures/Glycans/G40183QN"},{"id":"T11","span":{"begin":435,"end":439},"obj":"https://glytoucan.org/Structures/Glycans/G17077FL"},{"id":"T12","span":{"begin":435,"end":439},"obj":"https://glytoucan.org/Structures/Glycans/G18625KA"},{"id":"T13","span":{"begin":1180,"end":1183},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T14","span":{"begin":1180,"end":1183},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T15","span":{"begin":1250,"end":1253},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T16","span":{"begin":1250,"end":1253},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T17","span":{"begin":1257,"end":1260},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T18","span":{"begin":1257,"end":1260},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T19","span":{"begin":1372,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T20","span":{"begin":1372,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":299,"end":302},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T2","span":{"begin":413,"end":417},"obj":"http://www.glycoepitope.jp/epitopes/EP0056"},{"id":"T3","span":{"begin":419,"end":423},"obj":"http://www.glycoepitope.jp/epitopes/EP0059"},{"id":"T4","span":{"begin":425,"end":429},"obj":"http://www.glycoepitope.jp/epitopes/EP0067"},{"id":"T5","span":{"begin":435,"end":439},"obj":"http://www.glycoepitope.jp/epitopes/EP0069"},{"id":"T6","span":{"begin":1180,"end":1183},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T7","span":{"begin":1250,"end":1253},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T8","span":{"begin":1372,"end":1375},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":656,"end":659},"obj":"http://www.uniprot.org/uniprot/P20132"},{"id":"T2","span":{"begin":1020,"end":1023},"obj":"http://www.uniprot.org/uniprot/P20132"},{"id":"T3","span":{"begin":1312,"end":1315},"obj":"http://www.uniprot.org/uniprot/P20132"},{"id":"T4","span":{"begin":807,"end":828},"obj":"http://www.uniprot.org/uniprot/P68133"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1215,"end":1218},"obj":"http://www.uniprot.org/uniprot/Q99NH7"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":197,"end":204},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":272,"end":279},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/117980"},{"id":"T3","span":{"begin":1354,"end":1361},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/117980"},{"id":"T4","span":{"begin":1577,"end":1583},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T5","span":{"begin":1800,"end":1807},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T6","span":{"begin":1828,"end":1835},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":1215,"end":1218},"obj":"http://purl.obolibrary.org/obo/GO_0003904"},{"id":"T2","span":{"begin":1435,"end":1455},"obj":"http://purl.obolibrary.org/obo/GO_0004645"},{"id":"T3","span":{"begin":1435,"end":1457},"obj":"http://purl.obolibrary.org/obo/GO_0004645"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GO-MF

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":169,"end":178},"obj":"http://purl.obolibrary.org/obo/GO_0005829"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":197,"end":204},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T2","span":{"begin":1828,"end":1835},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T3","span":{"begin":1821,"end":1835},"obj":"http://purl.obolibrary.org/obo/UBERON_0002385"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":20,"end":28},"obj":"http://edamontology.org/topic_0078"},{"id":"T2","span":{"begin":89,"end":97},"obj":"http://edamontology.org/topic_0078"},{"id":"T3","span":{"begin":215,"end":222},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":363,"end":370},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":472,"end":479},"obj":"http://edamontology.org/topic_0078"},{"id":"T6","span":{"begin":717,"end":730},"obj":"http://edamontology.org/topic_0804"},{"id":"T7","span":{"begin":763,"end":770},"obj":"http://edamontology.org/topic_0078"},{"id":"T8","span":{"begin":902,"end":909},"obj":"http://edamontology.org/topic_0078"},{"id":"T9","span":{"begin":951,"end":958},"obj":"http://edamontology.org/topic_0078"},{"id":"T10","span":{"begin":1148,"end":1155},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":1192,"end":1199},"obj":"http://edamontology.org/topic_0078"},{"id":"T12","span":{"begin":1237,"end":1244},"obj":"http://edamontology.org/topic_0078"},{"id":"T13","span":{"begin":1273,"end":1280},"obj":"http://edamontology.org/topic_0078"},{"id":"T14","span":{"begin":1509,"end":1516},"obj":"http://edamontology.org/topic_0078"},{"id":"T15","span":{"begin":1597,"end":1604},"obj":"http://edamontology.org/topic_3678"},{"id":"T16","span":{"begin":1676,"end":1684},"obj":"http://edamontology.org/topic_0078"},{"id":"T17","span":{"begin":1749,"end":1757},"obj":"http://edamontology.org/topic_0078"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

EDAM-DFO

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T2","span":{"begin":53,"end":59},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T3","span":{"begin":146,"end":160},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T4","span":{"begin":154,"end":160},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T5","span":{"begin":807,"end":822},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T6","span":{"begin":816,"end":822},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T7","span":{"begin":830,"end":844},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T8","span":{"begin":838,"end":844},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T9","span":{"begin":929,"end":944},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T10","span":{"begin":938,"end":944},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T11","span":{"begin":1076,"end":1091},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T12","span":{"begin":1085,"end":1091},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T13","span":{"begin":1426,"end":1441},"obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"T14","span":{"begin":1435,"end":1441},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T15","span":{"begin":1690,"end":1696},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T16","span":{"begin":1821,"end":1827},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":290,"end":298},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":299,"end":302},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1180,"end":1183},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":1250,"end":1253},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":1372,"end":1375},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":413,"end":417},"obj":"http://www.glycoepitope.jp/epitopes/EP0056"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":419,"end":423},"obj":"http://www.glycoepitope.jp/epitopes/EP0059"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":425,"end":429},"obj":"http://www.glycoepitope.jp/epitopes/EP0067"},{"id":"PD-GlycoEpitope-B_T9","span":{"begin":435,"end":439},"obj":"http://www.glycoepitope.jp/epitopes/EP0069"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":197,"end":204},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1577,"end":1583},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1828,"end":1835},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1821,"end":1835},"obj":"http://purl.obolibrary.org/obo/UBERON_0002385"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

Glycan-GlyCosmos

GlyCosmos-GlycoEpitope

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":299,"end":302},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":413,"end":417},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":419,"end":423},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":425,"end":429},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":435,"end":439},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1180,"end":1183},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1250,"end":1253},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1372,"end":1375},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0056"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0059"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0067"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0069"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlyCosmos15-NCBITAXON

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":122,"end":132},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":272,"end":279},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1354,"end":1361},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10141"},{"id":"A2","pred":"db_id","subj":"T2","obj":"117980"},{"id":"A3","pred":"db_id","subj":"T3","obj":"117980"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlyCosmos15-UBERON

GlyCosmos15-MAT

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"Body_part"},{"id":"T2","span":{"begin":146,"end":160},"obj":"Body_part"},{"id":"T3","span":{"begin":807,"end":822},"obj":"Body_part"},{"id":"T4","span":{"begin":830,"end":844},"obj":"Body_part"},{"id":"T5","span":{"begin":929,"end":944},"obj":"Body_part"},{"id":"T6","span":{"begin":1076,"end":1091},"obj":"Body_part"},{"id":"T7","span":{"begin":1426,"end":1441},"obj":"Body_part"},{"id":"T8","span":{"begin":1690,"end":1696},"obj":"Body_part"},{"id":"T9","span":{"begin":1821,"end":1827},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000025"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

sentences

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":60},"obj":"Sentence"},{"id":"T2","span":{"begin":61,"end":161},"obj":"Sentence"},{"id":"T3","span":{"begin":162,"end":303},"obj":"Sentence"},{"id":"T4","span":{"begin":304,"end":380},"obj":"Sentence"},{"id":"T5","span":{"begin":381,"end":460},"obj":"Sentence"},{"id":"T6","span":{"begin":461,"end":679},"obj":"Sentence"},{"id":"T7","span":{"begin":680,"end":829},"obj":"Sentence"},{"id":"T8","span":{"begin":830,"end":945},"obj":"Sentence"},{"id":"T9","span":{"begin":946,"end":1029},"obj":"Sentence"},{"id":"T10","span":{"begin":1030,"end":1156},"obj":"Sentence"},{"id":"T11","span":{"begin":1157,"end":1261},"obj":"Sentence"},{"id":"T12","span":{"begin":1262,"end":1321},"obj":"Sentence"},{"id":"T13","span":{"begin":1322,"end":1472},"obj":"Sentence"},{"id":"T14","span":{"begin":1473,"end":1576},"obj":"Sentence"},{"id":"T15","span":{"begin":1577,"end":1706},"obj":"Sentence"},{"id":"T16","span":{"begin":1707,"end":1836},"obj":"Sentence"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

GlyCosmos15-Glycan

GlyCosmos15-GlycoEpitope

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":299,"end":302},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":413,"end":417},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":419,"end":423},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":425,"end":429},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":435,"end":439},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1180,"end":1183},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1250,"end":1253},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1372,"end":1375},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0056"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0059"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0067"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0069"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":122,"end":132},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":272,"end":279},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1354,"end":1361},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10141"},{"id":"A2","pred":"db_id","subj":"T2","obj":"117980"},{"id":"A3","pred":"db_id","subj":"T3","obj":"117980"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"Body_part"},{"id":"T2","span":{"begin":146,"end":160},"obj":"Body_part"},{"id":"T3","span":{"begin":807,"end":822},"obj":"Body_part"},{"id":"T4","span":{"begin":830,"end":844},"obj":"Body_part"},{"id":"T5","span":{"begin":929,"end":944},"obj":"Body_part"},{"id":"T6","span":{"begin":1076,"end":1091},"obj":"Body_part"},{"id":"T7","span":{"begin":1426,"end":1441},"obj":"Body_part"},{"id":"T8","span":{"begin":1690,"end":1696},"obj":"Body_part"},{"id":"T9","span":{"begin":1821,"end":1827},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000302"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000025"}],"text":"Ganglioside-binding proteins in skeletal and cardiac muscle.\nSeveral ganglioside-binding proteins have been identified in guinea pig skeletal and cardiac muscle. In the cytosolic fractions of both tissues, a 130-kD protein was found to have the highest propensity to bind lucifer yellow CH-labelled GM1. This binding could be abolished by prior incubation of the protein with GM2. Polysialogangliosides including GD1a, GD1b, GT1b, and GQ1b were less effective. The 130-kD protein migrated as a doublet with apparent isoelectric points (pI) of 6.3 and 6.5, respectively, in isoelectric focusing gel, but as a single species with an apparent Mr of 43,000 in SDS-polyacrylamide gel. Both the ganglioside-binding and the immunological properties of the 43-kD subunit protein were different from those of rabbit skeletal muscle actin. Cardiac muscle extract also contained a 77-kD minor ganglioside-binding protein that was absent in skeletal muscle. This protein had an apparent pI of 5.4 and migrated as a 39-kD species in SDS gels. By contrast, only the particulate fraction of skeletal muscle was found to contain a 180-kD major ganglioside-binding protein. Binding of fluorescent GM1 to this protein was blocked by pre-incubation of the protein with GM1 or GM2. The 180-kD protein migrated as a 98-kD species in SDS gels. However, its propensity to bind lucifer yellow CH-GM1 was at least 10 times greater than that of rabbit skeletal muscle phosphorylase b (Mr = 97,400). The apparent pI (6.5) of the 180-kD protein also was slightly higher than that of rabbit phosphorylase. Tissue distribution studies revealed that both the 130-kD and the 180-kD major ganglioside-binding proteins were muscle specific. It is, therefore, possible that these two proteins may play some unique roles in ganglioside-related functions in muscle tissues."}

Anatomy-UBERON