Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance |
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| Authors: | Benitez Maria J. Mier Gerardo Brione Fernando Moreno Francisco J. Jimémez Juan S. |
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| Affiliation: | (1) Departamento de Químíca Física Aplicada, Universidad Aut´noma de Madrid, Madrid, Spain;(2) Centro Nacional de Microelectrónica (CSIC), Madrid, Spain;(3) Centro de Biología Molecular Severo Ochoa (UAM-CSIC), Universidad Autónorna de Madrid, Madrid, Spain |
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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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| Keywords: | CK2 polylysine Surface Plasmon Research |
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