Abstract
Radioactive preparations of polyoma virus purified by treatment with ribonuclease and deoxyribonuclease, fluorocarbon extraction, and banding in rubidium chloride density gradients were found to be electrophoretically heterogeneous when examined by the sucrose-gradient zone electrophoresis method. Infectivity and hemagglutinin activity moved with the same negative mobility, constant in different preparations; other distinctly resolved radioactive components, probably consisting of DNA bound to cellular and viral material, also were generally found. Large-plaque virus migrated at about 1.5 times the speed of small plaque-virus at pH 8.5 and pH 7.2. “Empty” particle fractions from rubidium chloride gradients contained hemagglutinating components of similar mobility to those of the “full” particle fractions indicating that the capsid alone determines the electrophoretic properties of the virus particle. Attempts at further purification of “full” band preparations were made. Treatment with trypsin released components which sedimented more slowly than the virus and gave virus preparations of increased electrophoretic homogeneity. Electrophoretic analysis of trypsin-treated preparations showed that transforming activity migrated at the same rate as plaque-forming activity.
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