Abstract
The nature of TMV mixed with RNase was investigated. No differences were found in the electrophoretic behavior or anion exchange chromatograms of TMV treated with RNase compared with that of TMV alone. However, the cationic character of the virus was changed by adding the enzyme.
The amount of TMV-RNase complex adsorbed to tobacco cell debris was not enhanced by the addition of phosphate in the medium, unlike the phosphate effect with TMV alone.
TMV mixed with RNase was very stable in the alkaline solution (pH 10), but a small portion of the TMV-RNase complex was degraded. Moreover, RNase did not stabilize the TMV protein polymer (rod) when the pH of the solution was raised from 5.9 to 7.6.
It was then discussed that the reduction of the virus infection by RNase might be caused by the changes in the adsorbing ability to the host and the structural stability of the virus.
