Abstract
Evidence has been accumulated which suggests that the control of transcription may involve the phosphorylation of nuclear proteins, in particular nonhistone proteins [l-3]. It was therefore interesting to compare the phosphoproteins of nuclear and nucleolar chromatins which show remarkable differences in template activity. In the preceding paper [4] we demonstrated the presence of a protein kinase activity in purified rat liver nucleoli. In this study the proteins of whole nuclei and isolated nucleoli were fractionated into saline-soluble and chromosomal proteins and the distribution of phosphoproteins was analyzed. Since up to now very little is known about the specificity of the phosphorylation reactions in vitro we compared the distribution of nuclear and nucleolar proteins labelled both in vivo and in vitro. [ 101.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
