Partial purification and biochemical characterization of herpesvirus saimiri

HVS propagated in Vero cells was labelled with 3H-leucine and purified by isopycnic flotation in sucrose. Electron microscopic examination revealed both complete and incomplete HVS. No significant contamination with cellular debris was noted. Polyacrylamide gel electrophoresis analysis of solubilized virus revealed at least 12 proteins varying in molecular weight from 8 000 to 200 000 daltons.