Association of a ribonuclease with the purified influenza virus

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Abstract
Purified influenza virus contains ribonuclease activity. The enzyme does not hydrolyze viral RNA but both 28 S and 18 S host cell RNA are degraded forming large (about 16 S) and small (about 5 S) fragments with the release of the acid-soluble material.It has an optimum temperature of 37 °C, requires no divalent ions, and is inhibited by 0.1 M EDTA and 1% SDS. Treatment with 4 M urea increases enzymatic activity considerably (42%) but is not a prerequisite for eliciting ribonuclease activity suggesting that the enzyme is probably located near the surface of the virus particle. Results show that the observed enzyme activity is virus-associated as no host cell protein is detectable in the purified virus.