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.
ASJC Scopus subject areas
- Molecular Biology