Abstract

Equine herpes virus purified from viremic serum of infected hamsters, either in sucrose or potassium tartrate gradients, can be further separated into an enveloped form (EF) and a membranous top component (MTC) by centrifugation in high salt-Tris-EDTA gradients. The polypeptides of sucrose purified virions, MTC, EF virions and nucleocapsids (purified in Renografin-76 density gradients) were analyzed by discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The EF virions were comprised of 28 polypeptides ranging in molecular weight from 276,000 to 16,000, 12 of them larger than 100,000. Sucrose purified virions and MTC were composed of a larger number of polypeptides, 50 and 38 respectively. Purified nucleocapsids contained five major structural proteins and six minor ones, these 11 nucleocapsid proteins ranged in molecular weight from 147,000 to 20,000.

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