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pubmed:abstractText |
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 the poly(A) polymerase previously described in reovirus (incubation at 43 degrees 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.
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