Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance.
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.
Benitez
M J
MJ
Departamento de Químíca Fisica Aplicada, Universidad Autónoma de Madrid, Spain.
Mier
G
G
Brione
F
F
Moreno
F J
FJ
Jiménez
J S
JS
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
D011107:Polylysine; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases