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Abstract
Abstract A very sensitive method for the detection of ribonuclease activity in tobacco mosaic virus (TMV) preparations is described. All TMV preparations that have been examined exhibit ribonuclease activity, the level of which depends on the method used for purifying the virus. Protein isolated from the virus also shows this activity. The ribonuclease has a pH optimum in the range 8.5–9.0, and its activity is not dependent on the presence of either magnesium or pyrophosphate. Attempts to remove the enzyme from TMV by additional steps of purification were partly successful. A nucleoprotein pellet prepared from healthy tobacco leaves by a procedure similar to that used for the preparation of TMV from infected leaves exhibits ribonuclease activity that has the same pH optimum as that of TMV preparations. It is concluded that the ribonuclease in TMV is not an integral part of the virus, but is probably due to the presence of host-plant particles, such as ribosomes, which are not completely removed during the isolation of the virus.
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