期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1974
卷号:71
期号:12
页码:4773-4777
DOI:10.1073/pnas.71.12.4773
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Poliovirus-infected HeLa cells were labeled with radioactive methionine or phenylalanine and subjected to a new purification procedure for the viral induced RNA polymerase activity. Detergent-solubilized polymerase activity was purified by precipitation with 2 M LiCl and sedimentation through sucrose gradients. Approximately 0.001% of the incorporated amino acid radio-activity sediments with the peak of polymerase activity. Gradient fractions comprising the polymerase activity peak were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and found to contain predominantly one virus-specific polypeptide. Polyacrylamide gel electrophoresis also reveals that this purified polypeptide migrates with a 58,000 molecular weight noncapsid polio-virus polypeptide.