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- W1534180278 abstract "Abstract A latent RNase was partially purified by ammonium sulfate fractionation and Sephadex G-75 gel filtration from rat reticulocyte lysate. By mixing free RNase and its inhibitor in vitro, the latent RNase was shown to be a complex of each component. The latent RNase was activated by SH reagents, but no dissociation of the complex was observed. It was also activated by 6 m urea and 0.1 m H2SO4, and in these cases the enzyme was released as judged by gel filtration. From the results of this and precious paper, a possible mechanism of the regulation of RNase activity in rat reticulocyte is discussed." @default.
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- W1534180278 date "1971-07-01" @default.
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- W1534180278 title "Degradation of RNA in rat reticulocytes" @default.
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- W1534180278 doi "https://doi.org/10.1016/0003-9861(71)90011-7" @default.
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