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Abstract
A microelectrophoresis technique has been used to study purified suspensions of buffalopox, vaccinia, variola and alastrim viruses. The electrophoretic behaviour of purified, but otherwise untreated buffalopox and vaccinia viruses was indistinguishable. Treatment with trypsin, lipase or p-toluene sulphonyl chloride altered the electrophoretic behaviour indicating that the virus surface is lipoprotein, but again, the viruses were indistinguishable. After treatment with 2-mercaptoethanol differences were found in the electrophoretic behaviour of buffalopox and vaccinia viruses. Preliminary experiments showed that cores, extracted from the viruses, also differed in electrophoretic behaviour.
The electrophoretic behaviour of variola virus was indistinguishable from that of alastrim virus even after treatment with 2-mercaptoethanol. However, further experiments indicated that the cores of these two viruses also differed in surface chemical composition.
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