@article{mbs:/content/journal/jgv/10.1099/0022-1317-27-1-101, author = "Brunt, A. A. and Barton, R. J. and Tremaine, J. H. and Stace-Smith, R.", title = "The Composition of Cauliflower Mosaic Virus Protein", journal= "Journal of General Virology", year = "1975", volume = "27", number = "1", pages = "101-106", doi = "https://doi.org/10.1099/0022-1317-27-1-101", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-27-1-101", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "SUMMARY Polyacrylamide-SDS gel electrophoresis indicated that cauliflower mosaic virus (CIMV) particles contain two major and possibly one minor structural polypeptides with mol. wt. of 68000, 42000 and 55000, respectively. Up to seven other minor bands produced by disrupted virus were probably degradation products or stable aggregates of the structural polypeptides. The amino acid composition of CIMV protein differs from that of most other plant viruses in containing about 18% lysine. The content of basic amino acids in CIMV protein suggests that at least one of the polypeptides is an internal component with a strong affinity for DNA.", }