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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1993-7-7
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pubmed:abstractText |
An 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11851-7
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:7685022-Chromatography, Affinity,
pubmed-meshheading:7685022-Chromatography, Gel,
pubmed-meshheading:7685022-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7685022-Molecular Weight,
pubmed-meshheading:7685022-Plant Viruses,
pubmed-meshheading:7685022-Plants,
pubmed-meshheading:7685022-RNA,
pubmed-meshheading:7685022-RNA Replicase,
pubmed-meshheading:7685022-Substrate Specificity
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pubmed:year |
1993
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pubmed:articleTitle |
RNA-directed RNA polymerase from tomato leaves. I. Purification and physical properties.
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Martinsried, Germany.
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pubmed:publicationType |
Journal Article
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