A poly(A) polymerase enzymic activity was found in partially purified preparations of a human rotavirus. The activity was demonstrated using conditions similar to those utilized for the detection of a poly(A) polymerase previously described in reovirus (incubation at 43 °C in 70 m-tris buffer pH 7.5 containing 12 m·Mn). The enzymic activity was associated only with complete, double-shelled particles. Characterization of the poly(A)-containing product of the reaction by gel filtration on Sephadex G-100, followed by chromatography on DEAE-cellulose in the presence of 7 -urea, showed that it is composed of oligonucleotides of a chain length similar to, or slightly larger than, those observed in reovirus.


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