@article{mbs:/content/journal/jgv/10.1099/0022-1317-64-10-2305, author = "Yee, Siu-Pok and Branton, Philip E.", title = "Co-purification of Protein Kinase Activity with the 58000 Dalton Polypeptide Coded for by the Early 1B Region of Human Adenovirus Type 5", journal= "Journal of General Virology", year = "1983", volume = "64", number = "10", pages = "2305-2309", doi = "https://doi.org/10.1099/0022-1317-64-10-2305", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-64-10-2305", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "Ad5", keywords = "58K protein", keywords = "protein kinase activity", keywords = "early protein", abstract = "SUMMARY Extracts from human adenovirus type 5 (Ad5)-transformed cells were fractionated by ammonium sulphate precipitation, DEAE-Sephacel chromatography and glycerol gradient centrifugation. In all cases, protein kinase activity co-purified with the 58000 mol. wt. polypeptide (58K) coded for by the early 1B region of Ad5. Kinase activity was also precipitated by an antiserum raised against a synthetic peptide corresponding to the predicted carboxy terminus of 58K. These data suggest that protein kinase activity is associated with 58K, either intrinsically or in an enzyme bound to 58K.", }