PubMed:7138860 JSONTXT

{"project":"Test-Species-PubTator","denotations":[{"id":"3","span":{"begin":20,"end":37},"obj":"Chemical"},{"id":"4","span":{"begin":38,"end":48},"obj":"Chemical"},{"id":"5","span":{"begin":52,"end":71},"obj":"Chemical"},{"id":"21","span":{"begin":136,"end":163},"obj":"Species"},{"id":"22","span":{"begin":267,"end":284},"obj":"Chemical"},{"id":"23","span":{"begin":285,"end":295},"obj":"Chemical"},{"id":"24","span":{"begin":313,"end":332},"obj":"Chemical"},{"id":"25","span":{"begin":344,"end":374},"obj":"Chemical"},{"id":"26","span":{"begin":376,"end":380},"obj":"Chemical"},{"id":"27","span":{"begin":417,"end":427},"obj":"Chemical"},{"id":"28","span":{"begin":542,"end":554},"obj":"Chemical"},{"id":"29","span":{"begin":567,"end":584},"obj":"Chemical"},{"id":"30","span":{"begin":646,"end":657},"obj":"Chemical"},{"id":"31","span":{"begin":666,"end":685},"obj":"Chemical"},{"id":"32","span":{"begin":888,"end":922},"obj":"Chemical"},{"id":"33","span":{"begin":924,"end":928},"obj":"Chemical"},{"id":"34","span":{"begin":972,"end":990},"obj":"Chemical"},{"id":"35","span":{"begin":1062,"end":1067},"obj":"Chemical"}],"attributes":[{"id":"A3","pred":"resolved_to","subj":"3","obj":"MESH:D006028"},{"id":"A4","pred":"resolved_to","subj":"4","obj":"MESH:C018835"},{"id":"A5","pred":"resolved_to","subj":"5","obj":"MESH:D010713"},{"id":"A22","pred":"resolved_to","subj":"22","obj":"MESH:D006028"},{"id":"A23","pred":"resolved_to","subj":"23","obj":"MESH:C018835"},{"id":"A24","pred":"resolved_to","subj":"24","obj":"MESH:D010713"},{"id":"A25","pred":"resolved_to","subj":"25","obj":"MESH:D004134"},{"id":"A26","pred":"resolved_to","subj":"26","obj":"MESH:D004134"},{"id":"A27","pred":"resolved_to","subj":"27","obj":"MESH:C018835"},{"id":"A28","pred":"resolved_to","subj":"28","obj":"MESH:D010743"},{"id":"A29","pred":"resolved_to","subj":"29","obj":"MESH:D006028"},{"id":"A30","pred":"resolved_to","subj":"30","obj":"MESH:D002784"},{"id":"A31","pred":"resolved_to","subj":"31","obj":"MESH:D010713"},{"id":"A32","pred":"resolved_to","subj":"32","obj":"MESH:C028694"},{"id":"A33","pred":"resolved_to","subj":"33","obj":"MESH:C028694"},{"id":"A34","pred":"resolved_to","subj":"34","obj":"MESH:D006028"},{"id":"A35","pred":"resolved_to","subj":"35","obj":"MESH:D008055"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"Test-Species-PubDictionaries","denotations":[{"id":"T1","span":{"begin":136,"end":152},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3988"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"Test-Species-PubDictionaries-PubMedBERT","denotations":[{"id":"T1","span":{"begin":38,"end":44},"obj":"Species"},{"id":"T2","span":{"begin":136,"end":152},"obj":"Species"},{"id":"T3","span":{"begin":198,"end":206},"obj":"Species"},{"id":"T4","span":{"begin":285,"end":291},"obj":"Species"},{"id":"T5","span":{"begin":417,"end":423},"obj":"Species"},{"id":"T6","span":{"begin":752,"end":756},"obj":"Species"},{"id":"T8","span":{"begin":824,"end":830},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"584403"},{"id":"A2","pred":"db_id","subj":"T2","obj":"3988"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1118549"},{"id":"A4","pred":"db_id","subj":"T4","obj":"584403"},{"id":"A5","pred":"db_id","subj":"T5","obj":"584403"},{"id":"A6","pred":"db_id","subj":"T6","obj":"689456"},{"id":"A7","pred":"db_id","subj":"T6","obj":"46988"},{"id":"A8","pred":"db_id","subj":"T8","obj":"584403"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":38,"end":48},"obj":"Glycan"},{"id":"T2","span":{"begin":285,"end":295},"obj":"Glycan"},{"id":"T3","span":{"begin":417,"end":427},"obj":"Glycan"},{"id":"T4","span":{"begin":824,"end":834},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G21856LC"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G21856LC"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":45,"end":48},"obj":"Glycan"},{"id":"T2","span":{"begin":292,"end":295},"obj":"Glycan"},{"id":"T3","span":{"begin":424,"end":427},"obj":"Glycan"},{"id":"T4","span":{"begin":831,"end":834},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":45,"end":48},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":292,"end":295},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":424,"end":427},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":831,"end":834},"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/EP0050"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":555,"end":561},"obj":"Body_part"},{"id":"T2","span":{"begin":924,"end":928},"obj":"Body_part"},{"id":"T3","span":{"begin":1125,"end":1134},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0004529"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0034889"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":136,"end":152},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3988"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"T2","span":{"begin":82,"end":343},"obj":"Sentence"},{"id":"T3","span":{"begin":344,"end":562},"obj":"Sentence"},{"id":"T4","span":{"begin":563,"end":778},"obj":"Sentence"},{"id":"T5","span":{"begin":779,"end":940},"obj":"Sentence"},{"id":"T6","span":{"begin":941,"end":1135},"obj":"Sentence"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":45,"end":48},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":292,"end":295},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":424,"end":427},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":831,"end":834},"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/EP0050"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":136,"end":152},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3988"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":555,"end":561},"obj":"Body_part"},{"id":"T2","span":{"begin":924,"end":928},"obj":"Body_part"},{"id":"T3","span":{"begin":1125,"end":1134},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0004529"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0034889"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A4","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A5","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":136,"end":163},"obj":"GL_000028"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":136,"end":163},"obj":"GL_000028"}],"text":"Organization of the glycosphingolipid asialo-GM1 in phosphatidylcholine bilayers.\nAn affinity purified monovalent ferritin conjugate of Ricinus communis agglutinin (RCA 60) is used with freeze-etch electron microscopy to study the ultrastructural localization of the glycosphingolipid asialo-GM1 in multilamellar phosphatidylcholine liposomes. Dimyristoylphosphatidylcholine (DMPC) liposomes containing up to 20 mol% asialo-GM1 and quenched below the main transition temperature show a striking linear localization of ferritin-RCA 60 between phospholipid ridges. The glycosphingolipid localization is similar to that postulated for up to 20 mol% cholesterol in pure phosphatidylcholine bilayers by Copeland, B.R. and McConnell, H.M. (Biochim. Biophys. Acta, 599, 95-109 (1980)). Above the main phase transition temperature, asialo-GM1 appears to be organized into clusters, especially in palmitoyloleoylphosphatidylcholine (POPC) liposomes. This clustered distribution of glycosphingolipids seen above the phase transition temperature suggests that this type of lipid may exhibit compositional domain structure in biological membranes."}