[Reversible dissociation of influenza virus ribonucleoprotein].
Dissociation of influenza virus RNP under the effect of salt was studied. Separation of RNA and protein components of influenza virus RNP was shown to occur in a linear 15-30% sucrose concentration gradient containing 1.1 M NaCl. Upon RNP dissociation, protein-protein interactions between individual molecules of the structural protein were retained. The sedimentation coefficient of the protein component was 52S. The possibility of reassociation of the RNA-protein complex was studied. More complete reassociation was observed to occur in the presence of 0.1 M NaCl. The resulting RNA-protein complex morphologically is similar to the native RNP of influenza virus.
D000818:Animals; D002499:Centrifugation, Density Gradient; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D009980:Influenza A virus / Q000032:analysis* / Q000648:ultrastructure; D008854:Microscopy, Electron; D012367:RNA, Viral / Q000032:analysis / Q000302:isolation & purification; D012261:Ribonucleoproteins / Q000032:analysis / Q000302:isolation & purification*; D014776:Virus Cultivation
D012367:RNA, Viral; D012261:Ribonucleoproteins
Obratimaia dissotsiatsiia ribonukleoproteida virusa grippa.