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- W2083192196 abstract "The particulate RNA polymerase activity (16 K sedimentable) was determined in virus-infected and uninfected tobacco, as well as after solubilization with Triton X-100. This enzyme activity was further purified by ammonium sulfate fractionation and density gradient centrifugation. The solubilized preparation obtained upon TNV infection represented an enzyme-template complex; in the course of purification somewhat variably increasing levels of dependence on added RNA were observed. RNA-dependent preparations obtained by density gradient centrifugation or polyethyleneglycol-dextran two phase separation had a molecular weight of approx 200,000. Purified enzyme preparations, upon SDS polyacrylamide gel electrophoresis, showed one predominant protein component with an approximate molecular weight of 60,000. The lower enzymatic activity in unifected tobacco was at all stages stimulated by, or dependent upon, added RNA, but otherwise showed very similar properties to that of TNV-infected plants. The activity, whether from infected or healthy plants, when free from endogenous template, was activated by all RNAs tested, with trunip yellow mosaic virus RNA and poly(AU) being the most active, and the RNAs of TNV and STNV no more active than other viral RNAs. The nature of this lack of specificity is discussed. The addition of STNV to the inoculum leads to diminished production of viruses and RNA polymerase." @default.
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- W2083192196 date "1976-07-01" @default.
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- W2083192196 title "RNA polymerase from tobacco necrosis virus infected and unifected tobacco. Purification of the membrane-associated enzyme" @default.
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- W2083192196 doi "https://doi.org/10.1016/0042-6822(76)90308-1" @default.
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