PubMed:7263639
Annnotations
Test-Species-PubTator
{"project":"Test-Species-PubTator","denotations":[{"id":"1","span":{"begin":90,"end":95},"obj":"Species"},{"id":"27","span":{"begin":148,"end":153},"obj":"Species"},{"id":"28","span":{"begin":195,"end":218},"obj":"Chemical"},{"id":"29","span":{"begin":345,"end":364},"obj":"Chemical"},{"id":"30","span":{"begin":370,"end":386},"obj":"Chemical"},{"id":"31","span":{"begin":391,"end":406},"obj":"Chemical"},{"id":"32","span":{"begin":415,"end":426},"obj":"Chemical"},{"id":"33","span":{"begin":498,"end":502},"obj":"Chemical"},{"id":"34","span":{"begin":710,"end":725},"obj":"Chemical"},{"id":"35","span":{"begin":910,"end":914},"obj":"Gene"},{"id":"36","span":{"begin":952,"end":957},"obj":"Gene"},{"id":"37","span":{"begin":1019,"end":1024},"obj":"Gene"},{"id":"38","span":{"begin":1035,"end":1052},"obj":"Chemical"},{"id":"39","span":{"begin":1056,"end":1060},"obj":"Gene"},{"id":"40","span":{"begin":1065,"end":1084},"obj":"Chemical"},{"id":"41","span":{"begin":1102,"end":1118},"obj":"Chemical"},{"id":"42","span":{"begin":1135,"end":1139},"obj":"Gene"},{"id":"43","span":{"begin":1150,"end":1167},"obj":"Chemical"},{"id":"44","span":{"begin":1188,"end":1205},"obj":"Chemical"},{"id":"45","span":{"begin":1209,"end":1214},"obj":"Gene"},{"id":"46","span":{"begin":1228,"end":1243},"obj":"Chemical"},{"id":"47","span":{"begin":1281,"end":1285},"obj":"Gene"},{"id":"48","span":{"begin":1290,"end":1295},"obj":"Gene"},{"id":"49","span":{"begin":1493,"end":1497},"obj":"Gene"},{"id":"50","span":{"begin":1506,"end":1511},"obj":"Gene"},{"id":"51","span":{"begin":1546,"end":1561},"obj":"Chemical"}],"attributes":[{"id":"A1","pred":"resolved_to","subj":"1","obj":"9606"},{"id":"A27","pred":"resolved_to","subj":"27","obj":"9606"},{"id":"A28","pred":"resolved_to","subj":"28","obj":"MESH:D019791"},{"id":"A29","pred":"resolved_to","subj":"29","obj":"MESH:D002809"},{"id":"A30","pred":"resolved_to","subj":"30","obj":"MESH:D003871"},{"id":"A31","pred":"resolved_to","subj":"31","obj":"MESH:D006497"},{"id":"A32","pred":"resolved_to","subj":"32","obj":"MESH:D006820"},{"id":"A33","pred":"resolved_to","subj":"33","obj":"MESH:C028019"},{"id":"A34","pred":"resolved_to","subj":"34","obj":"MESH:C035771"},{"id":"A35","pred":"resolved_to","subj":"35","obj":"633"},{"id":"A36","pred":"resolved_to","subj":"36","obj":"1634"},{"id":"A37","pred":"resolved_to","subj":"37","obj":"633"},{"id":"A38","pred":"resolved_to","subj":"38","obj":"MESH:D006025"},{"id":"A39","pred":"resolved_to","subj":"39","obj":"633"},{"id":"A40","pred":"resolved_to","subj":"40","obj":"MESH:D002809"},{"id":"A41","pred":"resolved_to","subj":"41","obj":"MESH:D003871"},{"id":"A42","pred":"resolved_to","subj":"42","obj":"633"},{"id":"A43","pred":"resolved_to","subj":"43","obj":"MESH:D006025"},{"id":"A44","pred":"resolved_to","subj":"44","obj":"MESH:D006025"},{"id":"A45","pred":"resolved_to","subj":"45","obj":"1634"},{"id":"A46","pred":"resolved_to","subj":"46","obj":"MESH:D006497"},{"id":"A47","pred":"resolved_to","subj":"47","obj":"633"},{"id":"A48","pred":"resolved_to","subj":"48","obj":"1634"},{"id":"A49","pred":"resolved_to","subj":"49","obj":"633"},{"id":"A50","pred":"resolved_to","subj":"50","obj":"1634"},{"id":"A51","pred":"resolved_to","subj":"51","obj":"MESH:D006820"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Test-Species-PubDictionaries
{"project":"Test-Species-PubDictionaries","denotations":[{"id":"T1","span":{"begin":90,"end":95},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":148,"end":153},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Test-Species-PubDictionaries-PubMedBERT
{"project":"Test-Species-PubDictionaries-PubMedBERT","denotations":[{"id":"T1","span":{"begin":90,"end":95},"obj":"Species"},{"id":"T2","span":{"begin":148,"end":153},"obj":"Species"},{"id":"T3","span":{"begin":370,"end":378},"obj":"Species"},{"id":"T4","span":{"begin":933,"end":939},"obj":"Species"},{"id":"T5","span":{"begin":975,"end":978},"obj":"Species"},{"id":"T6","span":{"begin":1029,"end":1034},"obj":"Species"},{"id":"T7","span":{"begin":1102,"end":1110},"obj":"Species"},{"id":"T8","span":{"begin":1297,"end":1301},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"2338555"},{"id":"A4","pred":"db_id","subj":"T4","obj":"48766"},{"id":"A5","pred":"db_id","subj":"T5","obj":"130404"},{"id":"A6","pred":"db_id","subj":"T6","obj":"1925465"},{"id":"A7","pred":"db_id","subj":"T7","obj":"2338555"},{"id":"A8","pred":"db_id","subj":"T8","obj":"1369087"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos6-Glycan-Motif-Image
{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1065,"end":1076},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
sentences
{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T2","span":{"begin":103,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":427},"obj":"Sentence"},{"id":"T4","span":{"begin":428,"end":663},"obj":"Sentence"},{"id":"T5","span":{"begin":664,"end":828},"obj":"Sentence"},{"id":"T6","span":{"begin":829,"end":987},"obj":"Sentence"},{"id":"T7","span":{"begin":988,"end":1024},"obj":"Sentence"},{"id":"T8","span":{"begin":1025,"end":1098},"obj":"Sentence"},{"id":"T9","span":{"begin":1099,"end":1227},"obj":"Sentence"},{"id":"T10","span":{"begin":1228,"end":1296},"obj":"Sentence"},{"id":"T11","span":{"begin":1297,"end":1393},"obj":"Sentence"},{"id":"T12","span":{"begin":1394,"end":1562},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T2","span":{"begin":103,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":427},"obj":"Sentence"},{"id":"T4","span":{"begin":428,"end":663},"obj":"Sentence"},{"id":"T5","span":{"begin":664,"end":828},"obj":"Sentence"},{"id":"T6","span":{"begin":829,"end":987},"obj":"Sentence"},{"id":"T7","span":{"begin":988,"end":1024},"obj":"Sentence"},{"id":"T8","span":{"begin":1025,"end":1098},"obj":"Sentence"},{"id":"T9","span":{"begin":1099,"end":1227},"obj":"Sentence"},{"id":"T10","span":{"begin":1228,"end":1296},"obj":"Sentence"},{"id":"T11","span":{"begin":1297,"end":1393},"obj":"Sentence"},{"id":"T12","span":{"begin":1394,"end":1562},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos6-Glycan-Motif-Structure
{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T2","span":{"begin":1065,"end":1076},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Glycosmos6-GlycoEpitope
{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":391,"end":406},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"T3","span":{"begin":1065,"end":1076},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T4","span":{"begin":1228,"end":1243},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Glycosmos6-MAT
{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"http://purl.obolibrary.org/obo/MAT_0000035"},{"id":"T2","span":{"begin":154,"end":159},"obj":"http://purl.obolibrary.org/obo/MAT_0000035"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-Glycan
{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"Glycan"},{"id":"T2","span":{"begin":1065,"end":1076},"obj":"Glycan"},{"id":"T4","span":{"begin":391,"end":406},"obj":"Glycan"},{"id":"T6","span":{"begin":1228,"end":1243},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Anatomy-MAT
{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"Body_part"},{"id":"T2","span":{"begin":154,"end":159},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000035"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000035"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Glycan-GlyCosmos
{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"Glycan"},{"id":"T2","span":{"begin":1065,"end":1076},"obj":"Glycan"},{"id":"T6","span":{"begin":391,"end":406},"obj":"Glycan"},{"id":"T4","span":{"begin":1228,"end":1243},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A4","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"},{"id":"A6","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G17927IW"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos-GlycoEpitope
{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":391,"end":406},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1065,"end":1076},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1228,"end":1243},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-UBERON
{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"Body_part"},{"id":"T2","span":{"begin":154,"end":159},"obj":"Body_part"},{"id":"T3","span":{"begin":160,"end":166},"obj":"Body_part"},{"id":"T4","span":{"begin":1381,"end":1392},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000947"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000947"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002523"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0004663"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-Taxon
{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":90,"end":95},"obj":"Organism"},{"id":"T2","span":{"begin":148,"end":153},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-Sentences
{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T2","span":{"begin":103,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":427},"obj":"Sentence"},{"id":"T4","span":{"begin":428,"end":663},"obj":"Sentence"},{"id":"T5","span":{"begin":664,"end":828},"obj":"Sentence"},{"id":"T6","span":{"begin":829,"end":987},"obj":"Sentence"},{"id":"T7","span":{"begin":988,"end":1098},"obj":"Sentence"},{"id":"T8","span":{"begin":1099,"end":1227},"obj":"Sentence"},{"id":"T9","span":{"begin":1228,"end":1296},"obj":"Sentence"},{"id":"T10","span":{"begin":1297,"end":1393},"obj":"Sentence"},{"id":"T11","span":{"begin":1394,"end":1562},"obj":"Sentence"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-GlycoEpitope
{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":345,"end":356},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":391,"end":406},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1065,"end":1076},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1228,"end":1243},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-FMA
{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"Body_part"},{"id":"T2","span":{"begin":154,"end":159},"obj":"Body_part"},{"id":"T3","span":{"begin":1381,"end":1392},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:3734"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:3734"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:14156"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
GlyCosmos15-MAT
{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"Body_part"},{"id":"T2","span":{"begin":154,"end":159},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000035"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000035"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
NCBITAXON
{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":90,"end":95},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":148,"end":153},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":96,"end":101},"obj":"Body_part"},{"id":"T2","span":{"begin":154,"end":159},"obj":"Body_part"},{"id":"T3","span":{"begin":160,"end":166},"obj":"Body_part"},{"id":"T4","span":{"begin":1381,"end":1392},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000947"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000947"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002523"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0004663"}],"text":"Isolation and preliminary characterization of proteoglycans dissociatively extracted from human aorta.\nAortic proteoglycans (PG) were isolated from human aorta intima-media preparations with 4 M guanidine hydrochloride in the presence of protease inhibitors. The extracted PG mixture comprised 67% of the total aortic PG and was composed of 65% chondroitin sulfate, 22% dermatan sulfate, 8% heparan sulfate, and 4% hyaluronate. Attempts at isolation and purification of PG monomers using isopycnic CsCl gradient centrifugation under associative and dissociative conditions resulted in appreciable loss of PG through associations with co-extracted aortic proteins. The addition of a gel chromatographic step on Sepharose CL-4B under dissociative conditions resulted in separation of PG from the majority of co-extracted proteins. In addition, the procedure resulted in a separation of the PG into a population (PG-I) eluting near the column V0 and one (PG-II) included with a Kav of 0.38. Hyaluronic acid co-eluted with PG-I. The major glycosaminoglycan in PG-I was chondroitin sulfate, (85 to 95%). No dermatan sulfate was detected in PG-I, but this glycosaminoglycan was the predominant glycosaminoglycan in PG-II (50 to 70%). Heparan sulfate was present in small amounts in both PG-I and PG-II. Data presented support the proposal of at least three species of PG monomers in the aortic wall. Chromatographic studies under dissociative and associative conditions indicated that PG comprising PG-I but not PG-II were capable of associations with hyaluronic acid."}