Abstract
The RNA bacteriophage R17 when exposed to pH 10.5 is disrupted to yield a protein and products of alkaline hydrolysis of the viral RNA. The protein has an intrinsic sedimentation coefficient of 41.1 s and an intrinsic viscosity of 0.055 dl./g at 20 °C. It has a typical protein absorbancy spectrum and contains less than 1% RNA. These data, together with electron micrographs, indicate that the protein consists of a hollow protein shell similar in structure to the protein portion of R17.
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