Abstract
Purification of Sendai virus by using aluminum phosphate gel was studied to remove the host components which are derived from chick embryos and are hardly removable by fractional centrifugation. As a result, 10 mg of aluminum phosphate gel prepared under the standard condition was shown to adsorb almost 15,000 hemagglutinin units of the virus at maximum. The adsorption and elution occurred almost immediately at 4[degree]C whenever the pH and salt concentrations of the medium were optimal. When the virus adsorbed to a large amount of gel was eluted fractionally with 0.25 [image] phosphate buffer of pH 8.0, highly purified virus, in the sense of hemagglutinin units per mg nitrogen, was constantly obtained. This value reached 682,000. The final fraction revealed a single component of 1100 S in the sedimentation pattern. Specificity of viral protein in the behavior at the time of adsorption and elution was discussed.
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