Abstract
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 mM-tris buffer pH 7.5 containing 12 mM·Mn2+). The enzymic activity was associated only with complete, double-shelled particles. Characterization of the poly(A)-containing product of the in vitro reaction by gel filtration on Sephadex G-100, followed by chromatography on DEAE-cellulose in the presence of 7 M-urea, showed that it is composed of oligonucleotides of a chain length similar to, or slightly larger than, those observed in reovirus.
† Present address: Department of Microbiology and Immunology, Duke University Medical Center, Box 3020, Durham, North Carolina 27710, U.S.A.