title: Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance.
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.
authors: Departamento de Químíca Fisica Aplicada, Universidad Autónoma de Madrid, Spain.
authors: M J
authors: MJ
authors: Benitez
authors: G
authors: G
authors: Mier
authors: F
authors: F
authors: Brione
authors: F J
authors: FJ
authors: Moreno
authors: J S
authors: JS
authors: Jiménez
mesh_terms: D047390:Casein Kinase II; D004789:Enzyme Activation; D007700:Kinetics; D011107:Polylysine / Q000378:metabolism*; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D020349:Surface Plasmon Resonance
chemical_list: D011107:Polylysine; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases