Abstract
A high molecular weight crystalline protein, possessing the properties of ring spot virus and differing markedly from tobacco mosaic virus protein in its physical, chemical and serological properties, has been isolated by means of an ultracentrifuge from Turkish tobacco plants diseased with tobacco ring spot virus. Ultracentrifugal methods were also used to demonstrate that high molecular weight proteins are characteristic of other virus diseases. The concentration of the different virus proteins in the host was found to differ greatly. The quantity ultracentrifuge, used in conjunction with an analytical ultracentrifuge, has proven to be a powerful tool for the concentration, purification and crystallization of high molecular weight virus proteins and to be indispensable in the case of unstable viruses existing in low concentration in the host.
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