PubMed:3929841 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":181,"end":183},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004120"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":42,"end":50},"obj":"Glycan"},{"id":"T2","span":{"begin":125,"end":133},"obj":"Glycan"},{"id":"T3","span":{"begin":369,"end":377},"obj":"Glycan"},{"id":"T4","span":{"begin":608,"end":616},"obj":"Glycan"},{"id":"T5","span":{"begin":671,"end":679},"obj":"Glycan"},{"id":"T6","span":{"begin":751,"end":759},"obj":"Glycan"},{"id":"T7","span":{"begin":944,"end":952},"obj":"Glycan"},{"id":"T8","span":{"begin":1119,"end":1127},"obj":"Glycan"},{"id":"T9","span":{"begin":1178,"end":1186},"obj":"Glycan"},{"id":"T10","span":{"begin":1234,"end":1242},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":42,"end":50},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":125,"end":133},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":369,"end":377},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":608,"end":616},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":671,"end":679},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":751,"end":759},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":944,"end":952},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1119,"end":1127},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1178,"end":1186},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1234,"end":1242},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0024"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":779,"end":784},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":974,"end":979},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":181,"end":183},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004120"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":306,"end":310},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000025"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":68},"obj":"Sentence"},{"id":"T2","span":{"begin":69,"end":264},"obj":"Sentence"},{"id":"T3","span":{"begin":265,"end":454},"obj":"Sentence"},{"id":"T4","span":{"begin":455,"end":617},"obj":"Sentence"},{"id":"T5","span":{"begin":618,"end":725},"obj":"Sentence"},{"id":"T6","span":{"begin":726,"end":986},"obj":"Sentence"},{"id":"T7","span":{"begin":987,"end":1195},"obj":"Sentence"},{"id":"T8","span":{"begin":1196,"end":1341},"obj":"Sentence"},{"id":"T9","span":{"begin":1342,"end":1441},"obj":"Sentence"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":42,"end":50},"obj":"Glycan"},{"id":"T2","span":{"begin":125,"end":133},"obj":"Glycan"},{"id":"T3","span":{"begin":369,"end":377},"obj":"Glycan"},{"id":"T4","span":{"begin":608,"end":616},"obj":"Glycan"},{"id":"T5","span":{"begin":671,"end":679},"obj":"Glycan"},{"id":"T6","span":{"begin":751,"end":759},"obj":"Glycan"},{"id":"T7","span":{"begin":944,"end":952},"obj":"Glycan"},{"id":"T8","span":{"begin":1119,"end":1127},"obj":"Glycan"},{"id":"T9","span":{"begin":1178,"end":1186},"obj":"Glycan"},{"id":"T10","span":{"begin":1234,"end":1242},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G61730RY"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":42,"end":50},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":125,"end":133},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":369,"end":377},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":608,"end":616},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":671,"end":679},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":751,"end":759},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":944,"end":952},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1119,"end":1127},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1178,"end":1186},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1234,"end":1242},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0024"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0024"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":779,"end":784},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":974,"end":979},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":306,"end":310},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000025"}],"text":"Enzyme immunoassay of 6-ketoprostaglandin F1 alpha in a solid phase.\nA solid-phase enzyme immunoassay of 6-ketoprostaglandin F1 alpha (a stable degradation product of prostaglandin I2) was developed in which the hapten molecule was labeled with beta-galactosidase. The antiserum was bound to a polystyrene tube, and the enzyme-labeled and unlabeled 6-ketoprostaglandin F1 alpha were allowed to react in a competitive manner with the immobilized antibody. The activity of the immunologically bound beta-galactosidase was assayed by fluorometry, and correlated with the amount of unlabeled 6-ketoprostaglandin F1 alpha. According to a calibration curve 6-ketoprostaglandin F1 alpha was detectable in a range of 30 fmol-10 pmol. When 6-ketoprostaglandin F1 alpha was extracted from human serum by using an octadecylsilyl silica column (Sep-Pak C18) and the crude extract was subjected to the enzyme immunoassay, the content of 6-ketoprostaglandin F1 alpha was 50-60 pmol/ml of human serum. An endogenous substance(s) which disturbed the immunoreaction and gave such an apparently high concentration of 6-ketoprostaglandin F1 alpha separated from the endogenous 6-ketoprostaglandin F1 alpha by HPLC. With the purified 6-ketoprostaglandin F1 alpha fraction there was a good correlation (r = 0.994) between enzyme immunoassay and radioimmunoassay. The validity of the enzyme immunoassay was confirmed by gas chromatography-selected ion monitoring."}