Soluble cAMP-independent protein kinase from human spleen (Journal article)

Gounaris, A./ Trangas, T. T./ Tsiapalis, C. M.


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.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών
Keywords: Adenosine Triphosphate/metabolism,Chromatography, Gel,Cyclic AMP/*metabolism,Guanosine Triphosphate/metabolism,Humans,Isoelectric Point,Kinetics,Molecular Weight,Protein Kinases/*metabolism,Spleen/*enzymology,Substrate Specificity
URI: http://olympias.lib.uoi.gr/jspui/handle/123456789/7473
ISSN: 0003-9861
Link: http://www.ncbi.nlm.nih.gov/pubmed/2827577
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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