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