抄録
The RNP was isolated from the liver microsomes of adult rat and the effect of urea on the dissociation and on the RNase activity of the RNP were examined.
1. Electrophoretic analysis showed that the RNP was hardly dissociated to free RNA and protein at pH 7.0 even in the concentrated urea solution, though it was gradually degraded to a slower component (component 3), of which RNA and protein are probably linked loosely by ionic bonds. This estimation is also supported by centrifugal analysis.
2. Paperchromatography in urea succeeded to demonstrate the dissociation of the RNP. When the RNP was developed in the concentrated urea solution, protein stained with bromphenol blue was always found at or near the starting line, while most RNA was detected near the solvent front. Eluted solutions from the paper, however, showed that this RNA contained considerable amount of Folin positive substances.
3. Either the autodegradation of the RNP and the RNase activity of the RNP were slightly activated by urea.
This work was supported by grants from the Wacksman Foundation in Japan.
