Antisera raised in rabbits against RK13 cells infected with herpes simplex virus type 1 were capable of specifically precipitating proteins synthesized after infection of BHK-21 cells with the virus. Analysis of these immune precipitates by polyacrylamide gel electrophoresis demonstrated ≧ 15 polypeptides with mol. wt. from 25 to 100000. A number of these polypeptides were not detected in purified preparations of virus particles.

Precipitates formed with two ‘monoprecipitin’ antisera were also analysed. Antiserum to the structural antigen Band II precipitated a major polypeptide of mol. wt. 47000, which was glycosylated, and corresponded in mobility to a minor component polypeptide of the herpes virus particle. The other monoprecipitin antiserum, to the herpes-specified thymidine kinase, precipitated a polypeptide with a mol. wt. of 44000. The thymidine kinase polypeptide was not glycosylated.


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