Abstract
Structures with RNA polymerase activity were isolated from influenza virus-infected cells, and consisted of ribonucleoprotein (RNP) complexes, similar in morphology to the viral internal component or nucleocapsid. The isolation procedure involved fractionation of infected cells in a discontinuous sucrose gradient, in which enzyme activity was concentrated in a fraction of intermediate density which contains both smooth and rough cytoplasmic membranes. The RNPs with polymerase activity were further purified in a velocity gradient, after which the peak fractions showed a 35-fold purification of the polymerase activity when compared with cytoplasmic extracts. The NP polypeptide, which is the subunit of the virion RNP, was the only virus-specific polypeptide detected in these RNP structures.
MeSH Terms
Animals
Carbon Isotopes
Cattle
Cell Fractionation
Cell Line
Centrifugation, Density Gradient
Cricetinae
Cytoplasm/enzymology
DNA-Directed RNA Polymerases/analysis,isolation & purification,metabolism
Electrophoresis, Polyacrylamide Gel
Glucosamine/metabolism
Kidney
Microscopy, Electron
Nucleoproteins/analysis
Nucleotides/metabolism
Orthomyxoviridae/analysis
Peptides/analysis
Protein Hydrolysates/metabolism
Staining and Labeling
Tritium
Viral Proteins/analysis
Chemicals
Carbon Isotopes
Nucleoproteins
Nucleotides
Peptides
Protein Hydrolysates
Viral Proteins
Tritium
DNA-Directed RNA Polymerases
Glucosamine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Compans R W
Caliguiri L A
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