Abstract
The aim of our study was to determine the total length of reovirus RNA and to better understand the breakage of this double-stranded RNA into smaller pieces. The protein-monolayer technique with urea as a denaturative agent was used in the study of reovirus RNA (type 3). In one series of experiments we incubated the purified virus in 4M urea at 4°C for 5 minutes prior to spreading. A spreadable protein (e. g., DFP-chymotrypsin) was then added to the incubation mixture which gave rise to a stable RNA-protein film on a 0.3M ammonium acetate subphase. After transfer to supports, measurement of the contrasted filaments revealed a tri-modal distribution, showing maximaz at 0.35μ, 0.70μ, and 1.15μ. (Figure 1). Filaments longer than 2.8μ were not observed. These results are in agreement with experiments in which phenol or sodium perchlorate extraction was used, but are discrepant from experiments involving urea extraction which show a peak at about 5μ length.
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