[Study of the structural polypeptides of Chilo suppressalis iridescent virus (Iridovirus type 6)].

We report a procedure for the purification of Chilo iridescent virus (Iridovirus type 6), an evaluation of the purification procedure, and the results of analyses of the virion proteins by acrylamide gel electrophoresis. Purity was evaluated in three ways, i.e., by analysis of purified virions from artificial mixtures of infected and labeled uninfected larvae, electrophoresis at neutral pH, and electron-microscopic examination. Analysis of the polypeptides of purified CIV gave the following results: (i) after solubilization with SDS-B-mercaptoethanol, 16 polypeptides could be resolved in Coomassie brillant blue-stained electrophoretograms with molecular weights ranging from 18,000 to 115,000; (ii) after solubilization with SDS-urea, 26 polypeptides could be resolved with molecular weights ranging from 10,000 to 230,000 daltons.