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

AuthorsBenítez, María J.; Mier, Gerardo; Briones Fernández-Pola, Fernando ; Moreno, Francisco J.; Jiménez, Juan S.
Surface Plasmon Research
Issue Date1999
CitationMolecular and Cellular Biochemistry 191 (1): 29-33 (1999)
AbstractThe 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.
Publisher version (URL)http://dx.doi.org/10.1023/A:1006821520346
Appears in Collections:(IMN-CNM) Artículos
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