Abstract
Purified Drosophila X virus (DXV) particles were analyzed. They band at a density of 1.345 g/ml in CsCl. The virion proteins were resolved into 6 major polypeptide species (MW 100,000, 50,000, 49,000, 44,000, 33,000 and 27,000) 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 2 equimolar fractions by polyacrylamide gel electrophoresis. The estimates of the MW of the 2 RNA species depends on their structure. If they exist as double-stranded molecules their electrophoretic mobility compared to that of reovirus type 3 RNA indicates for each species an average MW of 2.2 .times. 106.