Purification and Properties of the RNA Polymerase-Template Complex of an Influenza Virus

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Abstract
The enzyme-template complex of influenza RNA polymerase (fowl plague virus) was purified 200-fold. The sole virus component found in this preparation was RNP-antigen. All attempts to remove the internal template led to an irreversible loss of enzyme activity. The complex was essentially free of nucleases. It synthesized exclusively viral minus strand RNA and was unable to initiate more than one cycle of RNA synthesis. The lag phase at the beginning of RNA synthesis in vitro, present in crude enzyme preparations, was abolished with the purified complex. The enzyme was sensitive to sulfhydryl reagents and it was able to accept α-S-ATP in place of ATP.

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