Treatment of purified Newcastle disease virus (NDV) with Triton N101 to activate the virus particle RNA polymerase in the assay removed the glycoproteins and most of the phospholipid from the virus. The subvirus particles produced by the action of Triton N101 on virus had RNA polymerase activity, whereas purified NDV nucleocapsids did not. Apparently, either nucleocapsids did not contain the proteins essential for RNA polymerase activity, or the enzyme was denatured during the preparation of nucleocapsids. Incubation of several purified strains of NDV at 4 °C led to loss of polymerase activity which was regained on incubation at 37 °C. It is suggested that internal configurational changes in the virus particle were the most likely causes of these changes in enzyme activity on incubation at 4 °C and 37 °C.


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