Purified X virus (DXV) particles have been analysed. They band at a density of 1.345 g/ml in CsCl. The virion proteins have been resolved into six major polypeptide species (mol. wt. 100000, 50000, 49000, 44000, 33000 and 27000) by polyacrylamide gel electrophoresis. The RNA sediments at 5S and 14S in sucrose gradients. The 5S RNA is sensitive to pancreatic RNase and the 14S RNA is resistant in its native form and sensitive after denaturation. The 14S RNA can be resolved into two equimolar fractions by polyacrylamide gel electrophoresis. The estimates of the mol. wt. of the two RNA species depends upon their structure. If they exist as double-stranded molecules their electrophoretic mobility compared to that of reovirus type 3 RNAs indicates for each species an average mol. wt. of 2.2 × 10.


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