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 -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.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error