Influenza virus A was disrupted by deoxycholate, Triton X100 or ether extraction into ribonucleoprotein and envelope proteins. The ribonucleoprotein was resolved into a 70 s, a 60 s and a 50 s component by sucrose gradient sedimentation. Three components of viral ribonucleoprotein were also obtained by polyacrylamide gel electrophoresis. The buoyant density of the viral nucleoprotein was 1.265 g/ml. in a sucrose density-gradient. The ribonucleoprotein was relatively resistant to pronase. But the RNA of the ribonucleoproteins of influenza virus was degraded by RNase. Probably the same three ribonucleoprotein components were also detected in virus-infected cells about three hours after infection. Distinct components of the influenza virus nucleoprotein were found to contain distinct viral RNA's, suggesting that their heterogeneity is original and not an artifact of the isolation procedures used. © 1969.