PubMed:7685022 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":47},"obj":"Sentence"},{"id":"T2","span":{"begin":48,"end":50},"obj":"Sentence"},{"id":"T3","span":{"begin":51,"end":88},"obj":"Sentence"},{"id":"T4","span":{"begin":89,"end":208},"obj":"Sentence"},{"id":"T5","span":{"begin":209,"end":378},"obj":"Sentence"},{"id":"T6","span":{"begin":379,"end":525},"obj":"Sentence"},{"id":"T7","span":{"begin":526,"end":603},"obj":"Sentence"},{"id":"T8","span":{"begin":604,"end":805},"obj":"Sentence"},{"id":"T9","span":{"begin":806,"end":917},"obj":"Sentence"},{"id":"T10","span":{"begin":918,"end":998},"obj":"Sentence"},{"id":"T11","span":{"begin":999,"end":1185},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":47},"obj":"Sentence"},{"id":"T2","span":{"begin":48,"end":50},"obj":"Sentence"},{"id":"T3","span":{"begin":51,"end":88},"obj":"Sentence"},{"id":"T4","span":{"begin":89,"end":208},"obj":"Sentence"},{"id":"T5","span":{"begin":209,"end":378},"obj":"Sentence"},{"id":"T6","span":{"begin":379,"end":525},"obj":"Sentence"},{"id":"T7","span":{"begin":526,"end":603},"obj":"Sentence"},{"id":"T8","span":{"begin":604,"end":805},"obj":"Sentence"},{"id":"T9","span":{"begin":806,"end":917},"obj":"Sentence"},{"id":"T10","span":{"begin":918,"end":998},"obj":"Sentence"},{"id":"T11","span":{"begin":999,"end":1185},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1058,"end":1063},"obj":"http://purl.obolibrary.org/obo/MAT_0000358"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":637,"end":652},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0018952"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1058,"end":1063},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000358"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":1043,"end":1070},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"12892"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":157,"end":163},"obj":"Body_part"},{"id":"T2","span":{"begin":1058,"end":1063},"obj":"Body_part"},{"id":"T4","span":{"begin":1178,"end":1184},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0005346"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0005813"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.\nAn RNA-directed RNA polymerase (RdRP, EC 2.7.7.48) from tomato leaf tissue was purified to electrophoretic homogeneity. A terminal transferase activity that was found to cofractionate with RdRP from DEAE-Sepharose and DNA-cellulose columns was removed by chromatography on a Mono Q column. The highly purified RdRP exhibits a specific activity of 500 nmol x mg-1 x 30 min-1, which corresponds to a 100,000-fold enrichment of the enzyme. In buffer containing 50% glycerol, its activity decreased by about 15%/month. RdRP activity coincided with the silver staining intensity of a single 128-kDa polypeptide when the fractions eluted from the Mono Q column were analyzed by electrophoresis in a SDS-polyacrylamide gel. Its molecular mass and its sedimentation coefficient of 6.6 S indicate that RdRP is a nearly globular molecule. The catalytic activity of RdRP is resistant to alpha-amanitin and actinomycin D. In tomato leaves systemically infected with potato spindle tuber viroid, the activity of RdRP was found to be increased about 3-fold compared with RdRP isolated from healthy leaf tissue."}