Abstract
Purified preparations of turnip yellow mosaic virus devoid of natural top component release their ribonucleic acid on treatment with a buffer of pH 12 at 30 °C. This process takes place very rapidly and leaves, in addition to the ribonucleic acid, empty protein shells and protein fragments in the reaction mixture. The protein shells can be isolated by a simple differential centrifugation procedure. This shell material has been characterized by its ultraviolet absorption spectrum, by sedimentation analysis, by diffusion, electrophoresis, electron microscopy, crystallization and X-ray diffraction, and has thus been shown to be identical with natural top component.
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