These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Protein kinase, phosphatase and protease activities in a fraction of RNA-binding proteins].
    Author: Kandror KV, Stepanov AS.
    Journal: Biokhimiia; 1983 Oct; 48(10):1674-9. PubMed ID: 6196057.
    Abstract:
    The RNA-binding proteins from amphibian (Rana temporaria and Xenopus laevis) oocytes contain a cAMP-independent caseintype protein kinase activity. This enzyme can phosphorylate casein but does not phosphorylate histones. Using high voltage paper electrophoresis of acid hydrolysate of [32P]casein, it was found that P-O-phosphoserine and [32P]-O-phosphothreonine are formed via the phosphorylation reaction. Protein kinase retains the ability to bind poly(U) under physiological ionic strength values. It was shown that RNA-binding proteins do not contain any detectable forms of phosphatase or protease which might distort the results of phosphorylation of endogenous and exogenous substrates.
    [Abstract] [Full Text] [Related] [New Search]