PubMed:166995 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":259},"obj":"Sentence"},{"id":"T3","span":{"begin":260,"end":345},"obj":"Sentence"},{"id":"T4","span":{"begin":346,"end":438},"obj":"Sentence"},{"id":"T5","span":{"begin":439,"end":531},"obj":"Sentence"},{"id":"T6","span":{"begin":532,"end":728},"obj":"Sentence"},{"id":"T7","span":{"begin":729,"end":864},"obj":"Sentence"},{"id":"T8","span":{"begin":865,"end":1132},"obj":"Sentence"},{"id":"T9","span":{"begin":1133,"end":1223},"obj":"Sentence"},{"id":"T10","span":{"begin":1224,"end":1416},"obj":"Sentence"},{"id":"T11","span":{"begin":1417,"end":1632},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":259},"obj":"Sentence"},{"id":"T3","span":{"begin":260,"end":345},"obj":"Sentence"},{"id":"T4","span":{"begin":346,"end":438},"obj":"Sentence"},{"id":"T5","span":{"begin":439,"end":531},"obj":"Sentence"},{"id":"T6","span":{"begin":532,"end":728},"obj":"Sentence"},{"id":"T7","span":{"begin":729,"end":864},"obj":"Sentence"},{"id":"T8","span":{"begin":865,"end":1132},"obj":"Sentence"},{"id":"T9","span":{"begin":1133,"end":1223},"obj":"Sentence"},{"id":"T10","span":{"begin":1224,"end":1416},"obj":"Sentence"},{"id":"T11","span":{"begin":1417,"end":1632},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase.\nProstaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":50,"end":55},"obj":"http://purl.obolibrary.org/obo/MAT_0000036"},{"id":"T2","span":{"begin":147,"end":152},"obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase.\nProstaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":192,"end":196},"obj":"HP_0000365"}],"text":"Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase.\nProstaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":50,"end":55},"obj":"Body_part"},{"id":"T5","span":{"begin":147,"end":152},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"A4","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0015230"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"A8","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0015230"}],"text":"Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase.\nProstaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":50,"end":55},"obj":"Body_part"},{"id":"T2","span":{"begin":147,"end":152},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000036"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase.\nProstaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase."}