Abstract
Summary We report the results of analyses of virion proteins by acrylamide gel electrophoresis. Purity was evaluated in three ways, i. e. by reconstruction experiments, electrophoresis of purified virions artificially mixed with uninfected cell lysate and electrophoresis in non-dissociating conditions of freshly purified virions. Analysis of the polypeptides from purified LDV indicates that after solubilization with SDS-β-mercaptoethanol, 22 polypeptides could be resolved in Coomassie-brillant-blue- or silver-nitrate-stained electrophoretograms as well as in autoradiograms. The molecular weights ranged from 30,700 to 210,000. After chloramin T or lactoperoxidase iodination, we could tentatively localize some proteins in the virions.
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