Separations of A-protein of tobacco mosaic virus by electrophoresis on polyacrylamide gels of various concentrations gave clear resolution of several components. The pherograms which were obtained varied according to the particular A-protein preparation employed, but corresponded well with estimates of the state of aggregation of the preparations made by electron microscopy or by sedimentation in the analytical ultracentrifuge. These estimates together with the results of immunodiffusion studies and electron-microscopic observations on material eluted from the gels following electrophoresis enabled the various components in the pherograms to be correlated with the known stable aggregates of A-protein. The electrophoretic mobilities of the various aggregates differ and increase with increases in size of the aggregates.


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