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: Soluble cAMP-independent protein kinase from human spleen.
    Author: Gounaris A, Trangas TT, Tsiapalis CM.
    Journal: Arch Biochem Biophys; 1987 Dec; 259(2):473-80. PubMed ID: 2827577.
    Abstract:
    A protein kinase (EC 2.7.1.37) was purified 2000-fold, from the soluble protein fraction of human spleen cells, using ion-exchange chromatography, ammonium sulfate fractionation, and gel filtration. This rapid procedure yielded 30% of the initial activity and an enzyme preparation with specific activity of 62 nmol min-1 mg-1 of protein. On the basis of disc gel electrophoresis in sodium dodecyl sulfate acrylamide gels and isoelectric focusing the enzyme preparation appears homogeneous and to consist of one polypeptide with a molecular weight of 43,000 and having a pI of 7.1. The purified enzyme activity is cyclic AMP and cGMP independent phosphorylates both alpha-casein and phosvitin, and uses Mg2+ ATP and Mg2+ GTP as phosphate donors, exhibiting an apparent Km of 2.0 and 6.6 X 10(-5)m, respectively. Furthermore, the enzyme activity is strongly inhibited by heparin (K50 = 0.1 micrograms/ml). These catalytic properties are characteristic of the enzyme casein kinase II, as described in several eukaryotic cells.
    [Abstract] [Full Text] [Related] [New Search]