Literature DB >> 173539

Nuclear protein kinases from murine cells.

J Schlepper, R Knippers.   

Abstract

Three protein kinase activities are found in nuclei from three different murine cells (Ehrlich ascites cells, mouse L cells and rat glioma cells). Two of these activities are soluble, one is bound to chromatin. The soluble enzymes are similar, if not identical, to the cytoplasmic protein kinases. The chromatin-bound, adenosine-cyclic-3':5'-monophosphate-independent enzyme is not found in the cytoplasm. This enzyme is composed of one subunit with a molecular weight of 80000-90000. Some biochemical properties of this enzyme are described. A brief description of a nuclear enzyme, which dephosphorylates phosphorylated histones, is also given.

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Year:  1975        PMID: 173539     DOI: 10.1111/j.1432-1033.1975.tb20993.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Binding of phosphorylated histone H1 to DNA.

Authors:  R Knippers; B Otto; R Böhme
Journal:  Nucleic Acids Res       Date:  1978-06       Impact factor: 16.971

Review 2.  Nuclear protein kinases.

Authors:  H R Matthews; V D Huebner
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

3.  Cyclin is a component of the sea urchin egg M-phase specific histone H1 kinase.

Authors:  L Meijer; D Arion; R Golsteyn; J Pines; L Brizuela; T Hunt; D Beach
Journal:  EMBO J       Date:  1989-08       Impact factor: 11.598

  3 in total

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