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Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance

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Abstract

The interaction between protein kinase CK2 and polylysine has been studied by Surface Plasmon Resonance (SPR). The binding process has a very low energy of activation, it is irreversible, and too slow as to explain the enzyme activity stimulation as a direct consequence of the polylysine binding. The polylysine interaction with a peptide substrate and with casein are faster, and in agreement with a substrate-mediated mechanism of activity stimulation. After several hours of incubation, the binding of polylysine to CK2 produces the loss of enzymatic activity.

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Authors and Affiliations

  1. Departamento de Químíca Física Aplicada, Universidad Aut´noma de Madrid, Madrid, Spain

    Maria J. Benitez

  2. Centro Nacional de Microelectrónica (CSIC), Madrid, Spain

    Gerardo Mier & Fernando Brione

  3. Centro de Biología Molecular Severo Ochoa (UAM-CSIC), Universidad Autónorna de Madrid, Madrid, Spain

    Francisco J. Moreno & Juan S. Jimémez

Authors
  1. Maria J. Benitez
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  2. Gerardo Mier
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  3. Fernando Brione
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  4. Francisco J. Moreno
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  5. Juan S. Jimémez
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Benitez, M.J., Mier, G., Brione, F. et al. Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance. Mol Cell Biochem 191, 29–33 (1999). https://doi.org/10.1023/A:1006821520346

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